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Lysine-specific demethylase 2A

Intermolecular
Cysteine 333 and cysteine 477
Intramolecular
Cysteine 574 and cysteine 577
Cysteine 574 and cysteine 609
Cysteine 571 and cysteine 574
Cysteine 642 and cysteine 675
Cysteine 642 and cysteine 645
Cysteine 582 and cysteine 585
Cysteine 585 and cysteine 604
Cysteine 620 and cysteine 623
Cysteine 585 and cysteine 588
More...
Cysteine 642 and cysteine 672
Cysteine 577 and cysteine 609
Cysteine 620 and cysteine 653
Cysteine 582 and cysteine 604
Cysteine 588 and cysteine 604
Cysteine 571 and cysteine 577
Cysteine 571 and cysteine 609
Cysteine 672 and cysteine 675
Cysteine 645 and cysteine 675
Cysteine 645 and cysteine 672
Cysteine 623 and cysteine 653
Cysteine 582 and cysteine 588
Cysteine 642 and cysteine 643
Cysteine 643 and cysteine 669
Cysteine 642 and cysteine 669
Cysteine 924 and cysteine 925
Cysteine 913 and cysteine 924
Cysteine 643 and cysteine 675
Cysteine 643 and cysteine 672
Cysteine 643 and cysteine 645
Cysteine 911 and cysteine 925
Cysteine 917 and cysteine 924
Cysteine 911 and cysteine 924
Cysteine 913 and cysteine 917
Cysteine 911 and cysteine 913
Cysteine 101 and cysteine 200
A redox-regulated disulphide may form between two units of Lysine-specific demethylase 2A at cysteines 333 and 477. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
4tn7
Structure name
crystal structure of mouse kdm2a-h3k36me-no complex
Structure deposition date
2014-06-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
69
Peptide A name
Lysine-specific demethylase 2A
Peptide B name
Lysine-specific demethylase 2A
Peptide A accession
P59997
Peptide B accession
P59997
Peptide A residue number
333
Peptide B residue number
477

Ligandability

Cysteine 333 of Lysine-specific demethylase 2A

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 477 of Lysine-specific demethylase 2A

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 2A between cysteines 574 and 577.

Details

Redox score ?
91
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
5
% buried
0
Peptide accession
Q9Y2K7
Residue number A
574
Residue number B
577
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 574 of Lysine-specific demethylase 2A

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 577 of Lysine-specific demethylase 2A

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 2A between cysteines 574 and 609.

Details

Redox score ?
89
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
5
% buried
0
Peptide accession
Q9Y2K7
Residue number A
574
Residue number B
609
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 574 of Lysine-specific demethylase 2A

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 2A

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 2A between cysteines 571 and 574.

Details

Redox score ?
89
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
5
% buried
0
Peptide accession
Q9Y2K7
Residue number A
571
Residue number B
574
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 571 of Lysine-specific demethylase 2A

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 574 of Lysine-specific demethylase 2A

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 2A between cysteines 642 and 675.

Details

Redox score ?
88
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
3
Peptide accession
Q9Y2K7
Residue number A
642
Residue number B
675
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 642 of Lysine-specific demethylase 2A

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 675 of Lysine-specific demethylase 2A

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 2A between cysteines 642 and 645.

Details

Redox score ?
88
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
5
% buried
3
Peptide accession
Q9Y2K7
Residue number A
642
Residue number B
645
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 642 of Lysine-specific demethylase 2A

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 645 of Lysine-specific demethylase 2A

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 2A between cysteines 582 and 585.

Details

Redox score ?
87
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
5
% buried
0
Peptide accession
Q9Y2K7
Residue number A
582
Residue number B
585
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 582 of Lysine-specific demethylase 2A

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 585 of Lysine-specific demethylase 2A

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 2A between cysteines 585 and 604.

Details

Redox score ?
87
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
5
% buried
0
Peptide accession
Q9Y2K7
Residue number A
585
Residue number B
604
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 585 of Lysine-specific demethylase 2A

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 604 of Lysine-specific demethylase 2A

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 2A between cysteines 620 and 623.

Details

Redox score ?
87
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
5
% buried
1
Peptide accession
Q9Y2K7
Residue number A
620
Residue number B
623
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 620 of Lysine-specific demethylase 2A

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 623 of Lysine-specific demethylase 2A

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 2A between cysteines 585 and 588.

Details

Redox score ?
87
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
5
% buried
0
Peptide accession
Q9Y2K7
Residue number A
585
Residue number B
588
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 585 of Lysine-specific demethylase 2A

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 588 of Lysine-specific demethylase 2A

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 2A between cysteines 642 and 672.

Details

Redox score ?
86
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
5
% buried
6
Peptide accession
Q9Y2K7
Residue number A
642
Residue number B
672
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 642 of Lysine-specific demethylase 2A

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 672 of Lysine-specific demethylase 2A

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 2A between cysteines 577 and 609.

Details

Redox score ?
86
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
0
Peptide accession
Q9Y2K7
Residue number A
577
Residue number B
609
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 577 of Lysine-specific demethylase 2A

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 2A

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 2A between cysteines 620 and 653.

Details

Redox score ?
86
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
6
Peptide accession
Q9Y2K7
Residue number A
620
Residue number B
653
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 620 of Lysine-specific demethylase 2A

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 653 of Lysine-specific demethylase 2A

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 2A between cysteines 582 and 604.

Details

Redox score ?
84
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
0
Peptide accession
Q9Y2K7
Residue number A
582
Residue number B
604
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 582 of Lysine-specific demethylase 2A

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 604 of Lysine-specific demethylase 2A

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 2A between cysteines 588 and 604.

Details

Redox score ?
84
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
7
% buried
0
Peptide accession
Q9Y2K7
Residue number A
588
Residue number B
604
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 588 of Lysine-specific demethylase 2A

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 604 of Lysine-specific demethylase 2A

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 2A between cysteines 571 and 577.

Details

Redox score ?
83
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
0
Peptide accession
Q9Y2K7
Residue number A
571
Residue number B
577
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 571 of Lysine-specific demethylase 2A

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 577 of Lysine-specific demethylase 2A

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 2A between cysteines 571 and 609.

Details

Redox score ?
83
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
0
Peptide accession
Q9Y2K7
Residue number A
571
Residue number B
609
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 571 of Lysine-specific demethylase 2A

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 2A

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 2A between cysteines 672 and 675.

Details

Redox score ?
81
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
6
Peptide accession
Q9Y2K7
Residue number A
672
Residue number B
675
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 672 of Lysine-specific demethylase 2A

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 675 of Lysine-specific demethylase 2A

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 2A between cysteines 645 and 675.

Details

Redox score ?
80
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
36
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y2K7
Residue number A
645
Residue number B
675
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 645 of Lysine-specific demethylase 2A

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 675 of Lysine-specific demethylase 2A

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 2A between cysteines 645 and 672.

Details

Redox score ?
80
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
2
Peptide accession
Q9Y2K7
Residue number A
645
Residue number B
672
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 645 of Lysine-specific demethylase 2A

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 672 of Lysine-specific demethylase 2A

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 2A between cysteines 623 and 653.

Details

Redox score ?
79
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
0
Peptide accession
Q9Y2K7
Residue number A
623
Residue number B
653
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 623 of Lysine-specific demethylase 2A

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 653 of Lysine-specific demethylase 2A

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 2A between cysteines 582 and 588.

Details

Redox score ?
78
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y2K7
Residue number A
582
Residue number B
588
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 582 of Lysine-specific demethylase 2A

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 588 of Lysine-specific demethylase 2A

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 2A between cysteines 642 and 643.

Details

Redox score ?
75
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
5
% buried
6
Peptide accession
Q9Y2K7
Residue number A
642
Residue number B
643
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 642 of Lysine-specific demethylase 2A

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 643 of Lysine-specific demethylase 2A

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 2A between cysteines 643 and 669.

Details

Redox score ?
72
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
8
Peptide accession
Q9Y2K7
Residue number A
643
Residue number B
669
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 643 of Lysine-specific demethylase 2A

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 669 of Lysine-specific demethylase 2A

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 2A between cysteines 642 and 669.

Details

Redox score ?
62
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
10
Peptide accession
Q9Y2K7
Residue number A
642
Residue number B
669
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 642 of Lysine-specific demethylase 2A

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 669 of Lysine-specific demethylase 2A

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 2A between cysteines 924 and 925.

Details

Redox score ?
61
PDB code
6c16
Structure name
ubiquitin variant (ubv
Structure deposition date
2018-01-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
11
Peptide accession
Q9Y2K7
Residue number A
924
Residue number B
925
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 924 of Lysine-specific demethylase 2A

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 925 of Lysine-specific demethylase 2A

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 2A between cysteines 913 and 924. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
6byh
Structure name
ubiquitin variant (ubv
Structure deposition date
2017-12-20
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
96
Peptide accession
Q9Y2K7
Residue number A
913
Residue number B
924
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 913 of Lysine-specific demethylase 2A

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 924 of Lysine-specific demethylase 2A

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 2A between cysteines 643 and 675. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y2K7
Residue number A
643
Residue number B
675
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 643 of Lysine-specific demethylase 2A

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 675 of Lysine-specific demethylase 2A

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 2A between cysteines 643 and 672. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
2
Peptide accession
Q9Y2K7
Residue number A
643
Residue number B
672
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 643 of Lysine-specific demethylase 2A

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 672 of Lysine-specific demethylase 2A

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 2A between cysteines 643 and 645. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4bbq
Structure name
crystal structure of the cxxc and phd domain of human lysine-specific demethylase 2a (kdm2a)(fbxl11)
Structure deposition date
2012-09-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y2K7
Residue number A
643
Residue number B
645
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 643 of Lysine-specific demethylase 2A

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 645 of Lysine-specific demethylase 2A

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 2A between cysteines 911 and 925. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
6byh
Structure name
ubiquitin variant (ubv
Structure deposition date
2017-12-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
8
Peptide accession
Q9Y2K7
Residue number A
911
Residue number B
925
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 911 of Lysine-specific demethylase 2A

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 925 of Lysine-specific demethylase 2A

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 2A between cysteines 917 and 924. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6byh
Structure name
ubiquitin variant (ubv
Structure deposition date
2017-12-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
68
Peptide accession
Q9Y2K7
Residue number A
917
Residue number B
924
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 917 of Lysine-specific demethylase 2A

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 924 of Lysine-specific demethylase 2A

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 2A between cysteines 911 and 924. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6byh
Structure name
ubiquitin variant (ubv
Structure deposition date
2017-12-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
60
Peptide accession
Q9Y2K7
Residue number A
911
Residue number B
924
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 911 of Lysine-specific demethylase 2A

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 924 of Lysine-specific demethylase 2A

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 2A between cysteines 913 and 917. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6byh
Structure name
ubiquitin variant (ubv
Structure deposition date
2017-12-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
74
Peptide accession
Q9Y2K7
Residue number A
913
Residue number B
917
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 913 of Lysine-specific demethylase 2A

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 917 of Lysine-specific demethylase 2A

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 2A between cysteines 911 and 913. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6byh
Structure name
ubiquitin variant (ubv
Structure deposition date
2017-12-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
56
Peptide accession
Q9Y2K7
Residue number A
911
Residue number B
913
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 911 of Lysine-specific demethylase 2A

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 913 of Lysine-specific demethylase 2A

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 2A between cysteines 101 and 200. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
4tn7
Structure name
crystal structure of mouse kdm2a-h3k36me-no complex
Structure deposition date
2014-06-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
64
Peptide accession
P59997
Residue number A
101
Residue number B
200
Peptide name
Lysine-specific demethylase 2A

Ligandability

Cysteine 101 of Lysine-specific demethylase 2A

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 200 of Lysine-specific demethylase 2A

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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