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Lysine-specific demethylase 2B

Intramolecular
Cysteine 616 and cysteine 619
Cysteine 619 and cysteine 651
Cysteine 613 and cysteine 651
Cysteine 616 and cysteine 651
Cysteine 662 and cysteine 665
Cysteine 630 and cysteine 646
Cysteine 627 and cysteine 630
Cysteine 691 and cysteine 722
Cysteine 624 and cysteine 646
Cysteine 624 and cysteine 627
More...
Cysteine 719 and cysteine 722
Cysteine 627 and cysteine 646
Cysteine 688 and cysteine 722
Cysteine 688 and cysteine 691
Cysteine 662 and cysteine 699
Cysteine 688 and cysteine 719
Cysteine 613 and cysteine 616
Cysteine 691 and cysteine 719
Cysteine 665 and cysteine 699
Cysteine 613 and cysteine 619
Cysteine 624 and cysteine 630
Cysteine 1085 and cysteine 1096
Cysteine 1278 and cysteine 1303
Cysteine 1248 and cysteine 1278
Cysteine 1285 and cysteine 1303
Cysteine 688 and cysteine 716
Cysteine 1089 and cysteine 1096
Cysteine 1285 and cysteine 1311
Cysteine 1303 and cysteine 1311
Cysteine 1096 and cysteine 1097
Cysteine 1083 and cysteine 1085
Cysteine 1083 and cysteine 1097
Cysteine 1168 and cysteine 1172
Cysteine 1085 and cysteine 1089
Cysteine 1083 and cysteine 1096
Cysteine 1278 and cysteine 1285
A redox-regulated disulphide may form within Lysine-specific demethylase 2B between cysteines 616 and 619.

Details

Redox score ?
78
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
616
Residue number B
619
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 616 of Lysine-specific demethylase 2B

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 619 of Lysine-specific demethylase 2B

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 2B between cysteines 619 and 651.

Details

Redox score ?
78
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
619
Residue number B
651
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 619 of Lysine-specific demethylase 2B

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 651 of Lysine-specific demethylase 2B

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 2B between cysteines 613 and 651.

Details

Redox score ?
77
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
613
Residue number B
651
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 613 of Lysine-specific demethylase 2B

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 651 of Lysine-specific demethylase 2B

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 2B between cysteines 616 and 651.

Details

Redox score ?
76
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
616
Residue number B
651
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 616 of Lysine-specific demethylase 2B

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 651 of Lysine-specific demethylase 2B

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 2B between cysteines 662 and 665.

Details

Redox score ?
76
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
662
Residue number B
665
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 662 of Lysine-specific demethylase 2B

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 665 of Lysine-specific demethylase 2B

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 2B between cysteines 630 and 646.

Details

Redox score ?
76
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
630
Residue number B
646
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 630 of Lysine-specific demethylase 2B

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 646 of Lysine-specific demethylase 2B

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 2B between cysteines 627 and 630.

Details

Redox score ?
76
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
627
Residue number B
630
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 627 of Lysine-specific demethylase 2B

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 630 of Lysine-specific demethylase 2B

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 2B between cysteines 691 and 722.

Details

Redox score ?
76
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
35
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
691
Residue number B
722
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 691 of Lysine-specific demethylase 2B

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 722 of Lysine-specific demethylase 2B

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 2B between cysteines 624 and 646.

Details

Redox score ?
75
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
624
Residue number B
646
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 624 of Lysine-specific demethylase 2B

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 646 of Lysine-specific demethylase 2B

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 2B between cysteines 624 and 627.

Details

Redox score ?
75
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
624
Residue number B
627
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 624 of Lysine-specific demethylase 2B

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 627 of Lysine-specific demethylase 2B

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 2B between cysteines 719 and 722.

Details

Redox score ?
75
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
719
Residue number B
722
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 719 of Lysine-specific demethylase 2B

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 722 of Lysine-specific demethylase 2B

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 2B between cysteines 627 and 646.

Details

Redox score ?
75
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
627
Residue number B
646
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 627 of Lysine-specific demethylase 2B

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 646 of Lysine-specific demethylase 2B

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 2B between cysteines 688 and 722.

Details

Redox score ?
75
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
688
Residue number B
722
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 688 of Lysine-specific demethylase 2B

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 722 of Lysine-specific demethylase 2B

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 2B between cysteines 688 and 691.

Details

Redox score ?
75
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
688
Residue number B
691
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 688 of Lysine-specific demethylase 2B

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 691 of Lysine-specific demethylase 2B

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 2B between cysteines 662 and 699.

Details

Redox score ?
74
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
662
Residue number B
699
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 662 of Lysine-specific demethylase 2B

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 2B

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 2B between cysteines 688 and 719.

Details

Redox score ?
74
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
688
Residue number B
719
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 688 of Lysine-specific demethylase 2B

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 719 of Lysine-specific demethylase 2B

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 2B between cysteines 613 and 616.

Details

Redox score ?
74
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
613
Residue number B
616
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 613 of Lysine-specific demethylase 2B

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 616 of Lysine-specific demethylase 2B

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 2B between cysteines 691 and 719.

Details

Redox score ?
74
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
691
Residue number B
719
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 691 of Lysine-specific demethylase 2B

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 719 of Lysine-specific demethylase 2B

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 2B between cysteines 665 and 699.

Details

Redox score ?
73
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
665
Residue number B
699
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 665 of Lysine-specific demethylase 2B

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 2B

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 2B between cysteines 613 and 619.

Details

Redox score ?
72
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
613
Residue number B
619
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 613 of Lysine-specific demethylase 2B

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 619 of Lysine-specific demethylase 2B

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 2B between cysteines 624 and 630.

Details

Redox score ?
72
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
624
Residue number B
630
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 624 of Lysine-specific demethylase 2B

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 630 of Lysine-specific demethylase 2B

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 2B between cysteines 1085 and 1096.

Details

Redox score ?
70
PDB code
5jh5
Structure name
structural basis for the hierarchical assembly of the core of prc1
Structure deposition date
2016-04-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
100
Peptide accession
Q8NHM5
Residue number A
1085
Residue number B
1096
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1085 of Lysine-specific demethylase 2B

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 1096 of Lysine-specific demethylase 2B

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 2B between cysteines 1278 and 1303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
5jh5
Structure name
structural basis for the hierarchical assembly of the core of prc1
Structure deposition date
2016-04-20
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
88
Peptide accession
Q8NHM5
Residue number A
1278
Residue number B
1303
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1278 of Lysine-specific demethylase 2B

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 1303 of Lysine-specific demethylase 2B

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 2B between cysteines 1248 and 1278. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
5jh5
Structure name
structural basis for the hierarchical assembly of the core of prc1
Structure deposition date
2016-04-20
Thiol separation (Å)
6
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
100
Peptide accession
Q8NHM5
Residue number A
1248
Residue number B
1278
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1248 of Lysine-specific demethylase 2B

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 1278 of Lysine-specific demethylase 2B

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 2B between cysteines 1285 and 1303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5jh5
Structure name
structural basis for the hierarchical assembly of the core of prc1
Structure deposition date
2016-04-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
87
Peptide accession
Q8NHM5
Residue number A
1285
Residue number B
1303
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1285 of Lysine-specific demethylase 2B

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 1303 of Lysine-specific demethylase 2B

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 2B between cysteines 688 and 716. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4o64
Structure name
zinc fingers of kdm2b
Structure deposition date
2013-12-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8NHM5
Residue number A
688
Residue number B
716
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 688 of Lysine-specific demethylase 2B

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 716 of Lysine-specific demethylase 2B

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 2B between cysteines 1089 and 1096. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6bva
Structure name
ubiquitin variant (ubv
Structure deposition date
2017-12-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
53
Peptide accession
Q8NHM5
Residue number A
1089
Residue number B
1096
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1089 of Lysine-specific demethylase 2B

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 1096 of Lysine-specific demethylase 2B

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 2B between cysteines 1285 and 1311. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
5jh5
Structure name
structural basis for the hierarchical assembly of the core of prc1
Structure deposition date
2016-04-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
77
Peptide accession
Q8NHM5
Residue number A
1285
Residue number B
1311
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1285 of Lysine-specific demethylase 2B

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 1311 of Lysine-specific demethylase 2B

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 2B between cysteines 1303 and 1311. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5jh5
Structure name
structural basis for the hierarchical assembly of the core of prc1
Structure deposition date
2016-04-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
67
Peptide accession
Q8NHM5
Residue number A
1303
Residue number B
1311
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1303 of Lysine-specific demethylase 2B

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 1311 of Lysine-specific demethylase 2B

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 2B between cysteines 1096 and 1097. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5jh5
Structure name
structural basis for the hierarchical assembly of the core of prc1
Structure deposition date
2016-04-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
82
Peptide accession
Q8NHM5
Residue number A
1096
Residue number B
1097
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1096 of Lysine-specific demethylase 2B

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 1097 of Lysine-specific demethylase 2B

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 2B between cysteines 1083 and 1085. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
5jh5
Structure name
structural basis for the hierarchical assembly of the core of prc1
Structure deposition date
2016-04-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
89
Peptide accession
Q8NHM5
Residue number A
1083
Residue number B
1085
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1083 of Lysine-specific demethylase 2B

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 1085 of Lysine-specific demethylase 2B

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 2B between cysteines 1083 and 1097. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
5jh5
Structure name
structural basis for the hierarchical assembly of the core of prc1
Structure deposition date
2016-04-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
71
Peptide accession
Q8NHM5
Residue number A
1083
Residue number B
1097
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1083 of Lysine-specific demethylase 2B

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 1097 of Lysine-specific demethylase 2B

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 2B between cysteines 1168 and 1172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5jh5
Structure name
structural basis for the hierarchical assembly of the core of prc1
Structure deposition date
2016-04-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
66
Peptide accession
Q8NHM5
Residue number A
1168
Residue number B
1172
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1168 of Lysine-specific demethylase 2B

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 1172 of Lysine-specific demethylase 2B

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 2B between cysteines 1085 and 1089. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6bva
Structure name
ubiquitin variant (ubv
Structure deposition date
2017-12-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
62
Peptide accession
Q8NHM5
Residue number A
1085
Residue number B
1089
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1085 of Lysine-specific demethylase 2B

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 1089 of Lysine-specific demethylase 2B

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 2B between cysteines 1083 and 1096. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
5jh5
Structure name
structural basis for the hierarchical assembly of the core of prc1
Structure deposition date
2016-04-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
89
Peptide accession
Q8NHM5
Residue number A
1083
Residue number B
1096
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1083 of Lysine-specific demethylase 2B

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 1096 of Lysine-specific demethylase 2B

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 2B between cysteines 1278 and 1285. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
5jh5
Structure name
structural basis for the hierarchical assembly of the core of prc1
Structure deposition date
2016-04-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
14
% buried
98
Peptide accession
Q8NHM5
Residue number A
1278
Residue number B
1285
Peptide name
Lysine-specific demethylase 2B

Ligandability

Cysteine 1278 of Lysine-specific demethylase 2B

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 1285 of Lysine-specific demethylase 2B

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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