ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Lysine-specific demethylase 6A

Intramolecular
Cysteine 1331 and cysteine 1358
Cysteine 1331 and cysteine 1361
Cysteine 1331 and cysteine 1334
Cysteine 1164 and cysteine 1234
Cysteine 1334 and cysteine 1361
Cysteine 1334 and cysteine 1358
Cysteine 1358 and cysteine 1361
Cysteine 900 and cysteine 1303
Cysteine 960 and cysteine 1153
Cysteine 1153 and cysteine 1247
A redox-regulated disulphide may form within Lysine-specific demethylase 6A between cysteines 1331 and 1358.

Details

Redox score ?
86
PDB code
3avr
Structure name
catalytic fragment of utx/kdm6a bound with histone h3k27me3 peptide, n-oxyalylglycine, and ni(ii)
Structure deposition date
2011-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
2
% buried
46
Peptide accession
O15550
Residue number A
1331
Residue number B
1358
Peptide name
Lysine-specific demethylase 6A

Ligandability

Cysteine 1331 of Lysine-specific demethylase 6A

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 1358 of Lysine-specific demethylase 6A

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 6A between cysteines 1331 and 1361.

Details

Redox score ?
84
PDB code
6fuk
Structure name
crystal structure of utx complexed with 5-carboxy-8-hydroxyquinoline
Structure deposition date
2018-02-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
5
% buried
21
Peptide accession
O15550
Residue number A
1331
Residue number B
1361
Peptide name
Lysine-specific demethylase 6A

Ligandability

Cysteine 1331 of Lysine-specific demethylase 6A

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 1361 of Lysine-specific demethylase 6A

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 6A between cysteines 1331 and 1334.

Details

Redox score ?
84
PDB code
6g8f
Structure name
crystal structure of utx complexed with gsk-j1
Structure deposition date
2018-04-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
5
% buried
26
Peptide accession
O15550
Residue number A
1331
Residue number B
1334
Peptide name
Lysine-specific demethylase 6A

Ligandability

Cysteine 1331 of Lysine-specific demethylase 6A

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 1334 of Lysine-specific demethylase 6A

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 6A between cysteines 1164 and 1234.

Details

Redox score ?
75
PDB code
6g8f
Structure name
crystal structure of utx complexed with gsk-j1
Structure deposition date
2018-04-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
7
% buried
98
Peptide accession
O15550
Residue number A
1164
Residue number B
1234
Peptide name
Lysine-specific demethylase 6A

Ligandability

Cysteine 1164 of Lysine-specific demethylase 6A

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 1234 of Lysine-specific demethylase 6A

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 6A between cysteines 1334 and 1361.

Details

Redox score ?
75
PDB code
3avr
Structure name
catalytic fragment of utx/kdm6a bound with histone h3k27me3 peptide, n-oxyalylglycine, and ni(ii)
Structure deposition date
2011-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
21
Peptide accession
O15550
Residue number A
1334
Residue number B
1361
Peptide name
Lysine-specific demethylase 6A

Ligandability

Cysteine 1334 of Lysine-specific demethylase 6A

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 1361 of Lysine-specific demethylase 6A

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 6A between cysteines 1334 and 1358.

Details

Redox score ?
74
PDB code
3avs
Structure name
catalytic fragment of utx/kdm6a bound with n-oxyalylglycine, and ni(ii)
Structure deposition date
2011-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
36
Peptide accession
O15550
Residue number A
1334
Residue number B
1358
Peptide name
Lysine-specific demethylase 6A

Ligandability

Cysteine 1334 of Lysine-specific demethylase 6A

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 1358 of Lysine-specific demethylase 6A

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 6A between cysteines 1358 and 1361.

Details

Redox score ?
72
PDB code
6ful
Structure name
crystal structure of utx complexed with 5-hydroxy-4-keto-1-methyl- picolinate
Structure deposition date
2018-02-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
28
Peptide accession
O15550
Residue number A
1358
Residue number B
1361
Peptide name
Lysine-specific demethylase 6A

Ligandability

Cysteine 1358 of Lysine-specific demethylase 6A

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 1361 of Lysine-specific demethylase 6A

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 6A between cysteines 900 and 1303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
6fuk
Structure name
crystal structure of utx complexed with 5-carboxy-8-hydroxyquinoline
Structure deposition date
2018-02-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
68
Peptide accession
O15550
Residue number A
900
Residue number B
1303
Peptide name
Lysine-specific demethylase 6A

Ligandability

Cysteine 900 of Lysine-specific demethylase 6A

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 6A

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 6A between cysteines 960 and 1153. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6ful
Structure name
crystal structure of utx complexed with 5-hydroxy-4-keto-1-methyl- picolinate
Structure deposition date
2018-02-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
96
Peptide accession
O15550
Residue number A
960
Residue number B
1153
Peptide name
Lysine-specific demethylase 6A

Ligandability

Cysteine 960 of Lysine-specific demethylase 6A

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 1153 of Lysine-specific demethylase 6A

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 6A between cysteines 1153 and 1247. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3avr
Structure name
catalytic fragment of utx/kdm6a bound with histone h3k27me3 peptide, n-oxyalylglycine, and ni(ii)
Structure deposition date
2011-03-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
10
% buried
74
Peptide accession
O15550
Residue number A
1153
Residue number B
1247
Peptide name
Lysine-specific demethylase 6A

Ligandability

Cysteine 1153 of Lysine-specific demethylase 6A

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 1247 of Lysine-specific demethylase 6A

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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