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Lysine-specific demethylase 5A

Intramolecular
Cysteine 679 and cysteine 699
Cysteine 676 and cysteine 699
Cysteine 676 and cysteine 679
Cysteine 690 and cysteine 709
Cysteine 1628 and cysteine 1655
Cysteine 1628 and cysteine 1658
Cysteine 1610 and cysteine 1615
Cysteine 1655 and cysteine 1658
Cysteine 692 and cysteine 707
Cysteine 337 and cysteine 340
More...
Cysteine 707 and cysteine 709
Cysteine 1632 and cysteine 1655
Cysteine 1615 and cysteine 1640
Cysteine 311 and cysteine 337
Cysteine 314 and cysteine 337
Cysteine 692 and cysteine 709
Cysteine 1628 and cysteine 1632
Cysteine 296 and cysteine 299
Cysteine 311 and cysteine 340
Cysteine 1632 and cysteine 1658
Cysteine 690 and cysteine 692
Cysteine 1610 and cysteine 1640
Cysteine 299 and cysteine 322
Cysteine 296 and cysteine 322
Cysteine 311 and cysteine 314
Cysteine 314 and cysteine 340
Cysteine 1615 and cysteine 1619
Cysteine 690 and cysteine 707
Cysteine 679 and cysteine 683
Cysteine 609 and cysteine 679
Cysteine 1610 and cysteine 1619
Cysteine 690 and cysteine 715
Cysteine 676 and cysteine 683
Cysteine 683 and cysteine 699
Cysteine 1610 and cysteine 1628
Cysteine 19 and cysteine 49
Cysteine 598 and cysteine 609
Cysteine 1610 and cysteine 1632
Cysteine 1610 and cysteine 1655
Cysteine 609 and cysteine 699
A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 679 and 699.

Details

Redox score ?
93
PDB code
5v9t
Structure name
crystal structure of selective pyrrolidine amide kdm5a inhibitor n- {(3r)-1-[3-(propan-2-yl)-1h-pyrazole-5-carbonyl]pyrrolidin-3- yl}cyclopropanecarboxamide (compound 48)
Structure deposition date
2017-03-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
66
Minimum pKa ?
1
% buried
60
Peptide accession
P29375
Residue number A
679
Residue number B
699
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 679 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 699 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 676 and 699.

Details

Redox score ?
91
PDB code
5k4l
Structure name
crystal structure of kdm5a in complex with a naphthyridone inhibitor
Structure deposition date
2016-05-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
69
Minimum pKa ?
0
% buried
72
Peptide accession
P29375
Residue number A
676
Residue number B
699
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 676 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 699 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 676 and 679.

Details

Redox score ?
90
PDB code
5v9t
Structure name
crystal structure of selective pyrrolidine amide kdm5a inhibitor n- {(3r)-1-[3-(propan-2-yl)-1h-pyrazole-5-carbonyl]pyrrolidin-3- yl}cyclopropanecarboxamide (compound 48)
Structure deposition date
2017-03-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
2
% buried
54
Peptide accession
P29375
Residue number A
676
Residue number B
679
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 676 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 679 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 690 and 709.

Details

Redox score ?
89
PDB code
5k4l
Structure name
crystal structure of kdm5a in complex with a naphthyridone inhibitor
Structure deposition date
2016-05-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
50
Minimum pKa ?
7
% buried
0
Peptide accession
P29375
Residue number A
690
Residue number B
709
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 690 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 709 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1628 and 1655.

Details

Redox score ?
88
PDB code
3gl6
Structure name
crystal structure of jarid1a-phd3 complexed with h3(1-9) k4me3 peptide
Structure deposition date
2009-03-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
6
% buried
0
Peptide accession
P29375
Residue number A
1628
Residue number B
1655
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1628 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1655 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1628 and 1658.

Details

Redox score ?
88
PDB code
3gl6
Structure name
crystal structure of jarid1a-phd3 complexed with h3(1-9) k4me3 peptide
Structure deposition date
2009-03-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
6
% buried
0
Peptide accession
P29375
Residue number A
1628
Residue number B
1658
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1628 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1658 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1610 and 1615 (3 and 8 respectively in this structure).

Details

Redox score ?
88
PDB code
5c11
Structure name
crystal structure of jarid1a phd finger bound to histone h3c4me3 peptide
Structure deposition date
2015-06-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
7
% buried
8
Peptide accession
P29375
Residue number A
1610
Residue number B
1615
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1610 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1615 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1655 and 1658.

Details

Redox score ?
87
PDB code
3gl6
Structure name
crystal structure of jarid1a-phd3 complexed with h3(1-9) k4me3 peptide
Structure deposition date
2009-03-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
8
% buried
0
Peptide accession
P29375
Residue number A
1655
Residue number B
1658
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1655 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1658 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 692 and 707.

Details

Redox score ?
87
PDB code
5v9p
Structure name
crystal structure of pyrrolidine amide inhibitor [(3s)-3-(4-bromo-1h- pyrazol-1-yl)pyrrolidin-1-yl][3-(propan-2-yl)-1h-pyrazol-5- yl]methanone (compound 35) in complex with kdm5a
Structure deposition date
2017-03-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
0
Peptide accession
P29375
Residue number A
692
Residue number B
707
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 692 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 707 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 337 and 340.

Details

Redox score ?
86
PDB code
7klo
Structure name
solution structure of the phd1 domain of histone demethylase kdm5a
Structure deposition date
2020-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
0
Peptide accession
P29375
Residue number A
337
Residue number B
340
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 337 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 340 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 707 and 709.

Details

Redox score ?
86
PDB code
5v9t
Structure name
crystal structure of selective pyrrolidine amide kdm5a inhibitor n- {(3r)-1-[3-(propan-2-yl)-1h-pyrazole-5-carbonyl]pyrrolidin-3- yl}cyclopropanecarboxamide (compound 48)
Structure deposition date
2017-03-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
7
% buried
0
Peptide accession
P29375
Residue number A
707
Residue number B
709
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 707 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 709 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1632 and 1655.

Details

Redox score ?
85
PDB code
3gl6
Structure name
crystal structure of jarid1a-phd3 complexed with h3(1-9) k4me3 peptide
Structure deposition date
2009-03-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
8
% buried
0
Peptide accession
P29375
Residue number A
1632
Residue number B
1655
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1632 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1655 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1615 and 1640 (8 and 33 respectively in this structure).

Details

Redox score ?
85
PDB code
5c11
Structure name
crystal structure of jarid1a phd finger bound to histone h3c4me3 peptide
Structure deposition date
2015-06-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
7
% buried
4
Peptide accession
P29375
Residue number A
1615
Residue number B
1640
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1615 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1640 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 311 and 337.

Details

Redox score ?
84
PDB code
7klo
Structure name
solution structure of the phd1 domain of histone demethylase kdm5a
Structure deposition date
2020-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
7
% buried
0
Peptide accession
P29375
Residue number A
311
Residue number B
337
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 311 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 337 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 314 and 337 (29 and 52 respectively in this structure).

Details

Redox score ?
83
PDB code
7klr
Structure name
solution structure of the phd1 domain of histone demethylase kdm5a in complex with a histone h3(1-10) peptide
Structure deposition date
2020-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
2
Peptide accession
P29375
Residue number A
314
Residue number B
337
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 314 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 337 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 692 and 709.

Details

Redox score ?
83
PDB code
5ceh
Structure name
structure of histone lysine demethylase kdm5a in complex with selective inhibitor
Structure deposition date
2015-07-06
Thiol separation (Å)
3
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
nan
Peptide accession
P29375
Residue number A
692
Residue number B
709
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 692 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 709 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1628 and 1632 (21 and 25 respectively in this structure).

Details

Redox score ?
83
PDB code
5c11
Structure name
crystal structure of jarid1a phd finger bound to histone h3c4me3 peptide
Structure deposition date
2015-06-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
1
Peptide accession
P29375
Residue number A
1628
Residue number B
1632
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1628 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1632 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 296 and 299 (11 and 14 respectively in this structure).

Details

Redox score ?
82
PDB code
7klr
Structure name
solution structure of the phd1 domain of histone demethylase kdm5a in complex with a histone h3(1-10) peptide
Structure deposition date
2020-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
8
Peptide accession
P29375
Residue number A
296
Residue number B
299
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 296 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 299 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 311 and 340 (26 and 55 respectively in this structure).

Details

Redox score ?
81
PDB code
7klr
Structure name
solution structure of the phd1 domain of histone demethylase kdm5a in complex with a histone h3(1-10) peptide
Structure deposition date
2020-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
6
Peptide accession
P29375
Residue number A
311
Residue number B
340
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 311 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 340 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1632 and 1658 (25 and 51 respectively in this structure).

Details

Redox score ?
81
PDB code
5c11
Structure name
crystal structure of jarid1a phd finger bound to histone h3c4me3 peptide
Structure deposition date
2015-06-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
31
Minimum pKa ?
9
% buried
0
Peptide accession
P29375
Residue number A
1632
Residue number B
1658
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1632 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1658 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 690 and 692.

Details

Redox score ?
81
PDB code
5v9t
Structure name
crystal structure of selective pyrrolidine amide kdm5a inhibitor n- {(3r)-1-[3-(propan-2-yl)-1h-pyrazole-5-carbonyl]pyrrolidin-3- yl}cyclopropanecarboxamide (compound 48)
Structure deposition date
2017-03-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
2
Peptide accession
P29375
Residue number A
690
Residue number B
692
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 690 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 692 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1610 and 1640 (3 and 33 respectively in this structure).

Details

Redox score ?
81
PDB code
5c11
Structure name
crystal structure of jarid1a phd finger bound to histone h3c4me3 peptide
Structure deposition date
2015-06-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
12
Peptide accession
P29375
Residue number A
1610
Residue number B
1640
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1610 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1640 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 299 and 322.

Details

Redox score ?
81
PDB code
7klo
Structure name
solution structure of the phd1 domain of histone demethylase kdm5a
Structure deposition date
2020-10-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
3
Peptide accession
P29375
Residue number A
299
Residue number B
322
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 299 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 322 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 296 and 322 (11 and 37 respectively in this structure).

Details

Redox score ?
81
PDB code
7klr
Structure name
solution structure of the phd1 domain of histone demethylase kdm5a in complex with a histone h3(1-10) peptide
Structure deposition date
2020-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
10
Peptide accession
P29375
Residue number A
296
Residue number B
322
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 296 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 322 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 311 and 314 (26 and 29 respectively in this structure).

Details

Redox score ?
80
PDB code
7klr
Structure name
solution structure of the phd1 domain of histone demethylase kdm5a in complex with a histone h3(1-10) peptide
Structure deposition date
2020-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
6
Peptide accession
P29375
Residue number A
311
Residue number B
314
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 311 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 314 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 314 and 340 (29 and 55 respectively in this structure).

Details

Redox score ?
78
PDB code
7klr
Structure name
solution structure of the phd1 domain of histone demethylase kdm5a in complex with a histone h3(1-10) peptide
Structure deposition date
2020-10-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
10
% buried
0
Peptide accession
P29375
Residue number A
314
Residue number B
340
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 314 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 340 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1615 and 1619.

Details

Redox score ?
78
PDB code
3gl6
Structure name
crystal structure of jarid1a-phd3 complexed with h3(1-9) k4me3 peptide
Structure deposition date
2009-03-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
26
Minimum pKa ?
7
% buried
0
Peptide accession
P29375
Residue number A
1615
Residue number B
1619
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1615 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1619 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 690 and 707.

Details

Redox score ?
76
PDB code
5ceh
Structure name
structure of histone lysine demethylase kdm5a in complex with selective inhibitor
Structure deposition date
2015-07-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
nan
Peptide accession
P29375
Residue number A
690
Residue number B
707
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 690 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 707 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 679 and 683.

Details

Redox score ?
66
PDB code
5v9t
Structure name
crystal structure of selective pyrrolidine amide kdm5a inhibitor n- {(3r)-1-[3-(propan-2-yl)-1h-pyrazole-5-carbonyl]pyrrolidin-3- yl}cyclopropanecarboxamide (compound 48)
Structure deposition date
2017-03-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
2
% buried
78
Peptide accession
P29375
Residue number A
679
Residue number B
683
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 679 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 683 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 609 and 679.

Details

Redox score ?
61
PDB code
5v9t
Structure name
crystal structure of selective pyrrolidine amide kdm5a inhibitor n- {(3r)-1-[3-(propan-2-yl)-1h-pyrazole-5-carbonyl]pyrrolidin-3- yl}cyclopropanecarboxamide (compound 48)
Structure deposition date
2017-03-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
2
% buried
70
Peptide accession
P29375
Residue number A
609
Residue number B
679
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 609 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 679 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1610 and 1619. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
3gl6
Structure name
crystal structure of jarid1a-phd3 complexed with h3(1-9) k4me3 peptide
Structure deposition date
2009-03-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
24
Minimum pKa ?
8
% buried
0
Peptide accession
P29375
Residue number A
1610
Residue number B
1619
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1610 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1619 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 690 and 715. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
5v9t
Structure name
crystal structure of selective pyrrolidine amide kdm5a inhibitor n- {(3r)-1-[3-(propan-2-yl)-1h-pyrazole-5-carbonyl]pyrrolidin-3- yl}cyclopropanecarboxamide (compound 48)
Structure deposition date
2017-03-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
7
% buried
18
Peptide accession
P29375
Residue number A
690
Residue number B
715
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 690 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 715 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 676 and 683. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
5ceh
Structure name
structure of histone lysine demethylase kdm5a in complex with selective inhibitor
Structure deposition date
2015-07-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
80
Peptide accession
P29375
Residue number A
676
Residue number B
683
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 676 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 683 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 683 and 699. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
5v9t
Structure name
crystal structure of selective pyrrolidine amide kdm5a inhibitor n- {(3r)-1-[3-(propan-2-yl)-1h-pyrazole-5-carbonyl]pyrrolidin-3- yl}cyclopropanecarboxamide (compound 48)
Structure deposition date
2017-03-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
84
Peptide accession
P29375
Residue number A
683
Residue number B
699
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 683 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 699 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1610 and 1628 (3 and 21 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2kgi
Structure name
solution structure of jarid1a c-terminal phd finger in complex with h3(1-9)k4me3
Structure deposition date
2009-03-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
18
Peptide accession
P29375
Residue number A
1610
Residue number B
1628
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1610 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1628 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 19 and 49. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6bgv
Structure name
linked kdm5a jmj domain bound to the inhibitor 2-((2-chlorophenyl)(2- (piperidin-1-yl)ethoxy)methyl)-1l2-pyrrolo[3,2-b]pyridine-7- carboxylic acid (compound n40)
Structure deposition date
2017-10-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
98
Peptide accession
P29375
Residue number A
19
Residue number B
49
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 19 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 49 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 598 and 609. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
5v9p
Structure name
crystal structure of pyrrolidine amide inhibitor [(3s)-3-(4-bromo-1h- pyrazol-1-yl)pyrrolidin-1-yl][3-(propan-2-yl)-1h-pyrazol-5- yl]methanone (compound 35) in complex with kdm5a
Structure deposition date
2017-03-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
88
Peptide accession
P29375
Residue number A
598
Residue number B
609
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 598 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 609 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1610 and 1632 (3 and 25 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2kgi
Structure name
solution structure of jarid1a c-terminal phd finger in complex with h3(1-9)k4me3
Structure deposition date
2009-03-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
13
Peptide accession
P29375
Residue number A
1610
Residue number B
1632
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1610 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1632 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 1610 and 1655 (3 and 48 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2kgi
Structure name
solution structure of jarid1a c-terminal phd finger in complex with h3(1-9)k4me3
Structure deposition date
2009-03-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
13
Peptide accession
P29375
Residue number A
1610
Residue number B
1655
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 1610 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 1655 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Lysine-specific demethylase 5A between cysteines 609 and 699. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
5ceh
Structure name
structure of histone lysine demethylase kdm5a in complex with selective inhibitor
Structure deposition date
2015-07-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
82
Peptide accession
P29375
Residue number A
609
Residue number B
699
Peptide name
Lysine-specific demethylase 5A

Ligandability

Cysteine 609 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 699 of Lysine-specific demethylase 5A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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