ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Histone lysine demethylase PHF8

Intermolecular
Cysteine 1299 of DNA topoisomerase 2-binding protein 1 and cysteine 844
Intramolecular
Cysteine 62 and cysteine 89
Cysteine 44 and cysteine 70
Cysteine 46 and cysteine 70
Cysteine 86 and cysteine 89
Cysteine 62 and cysteine 86
Cysteine 44 and cysteine 46
Cysteine 59 and cysteine 89
Cysteine 59 and cysteine 86
Cysteine 59 and cysteine 62
More...
Cysteine 44 and cysteine 86
Cysteine 271 and cysteine 363
A redox-regulated disulphide may form between cysteine 1299 of DNA topoisomerase 2-binding protein 1 and cysteine 844 of Histone lysine demethylase PHF8.

Details

Redox score ?
86
PDB code
7cmz
Structure name
crystal structure of brct7/8 in complex with the aps motif of phf8
Structure deposition date
2020-07-29
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide A name
DNA topoisomerase 2-binding protein 1
Peptide B name
Histone lysine demethylase PHF8
Peptide A accession
Q92547
Peptide B accession
Q9UPP1
Peptide A residue number
1299
Peptide B residue number
844

Ligandability

Cysteine 1299 of DNA topoisomerase 2-binding protein 1

Cysteine 844 of Histone lysine demethylase PHF8

A redox-regulated disulphide may form within Histone lysine demethylase PHF8 between cysteines 62 and 89 (26 and 53 respectively in this structure).

Details

Redox score ?
87
PDB code
3kv4
Structure name
structure of phf8 in complex with histone h3
Structure deposition date
2009-11-29
Thiol separation (Å)
3
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
7
Peptide accession
Q9UPP1
Residue number A
62
Residue number B
89
Peptide name
Histone lysine demethylase PHF8

Ligandability

Cysteine 62 of Histone lysine demethylase PHF8

Cysteine 89 of Histone lysine demethylase PHF8

A redox-regulated disulphide may form within Histone lysine demethylase PHF8 between cysteines 44 and 70 (8 and 34 respectively in this structure).

Details

Redox score ?
85
PDB code
3kv4
Structure name
structure of phf8 in complex with histone h3
Structure deposition date
2009-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
18
Peptide accession
Q9UPP1
Residue number A
44
Residue number B
70
Peptide name
Histone lysine demethylase PHF8

Ligandability

Cysteine 44 of Histone lysine demethylase PHF8

Cysteine 70 of Histone lysine demethylase PHF8

A redox-regulated disulphide may form within Histone lysine demethylase PHF8 between cysteines 46 and 70 (10 and 34 respectively in this structure).

Details

Redox score ?
83
PDB code
3kv4
Structure name
structure of phf8 in complex with histone h3
Structure deposition date
2009-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
6
% buried
4
Peptide accession
Q9UPP1
Residue number A
46
Residue number B
70
Peptide name
Histone lysine demethylase PHF8

Ligandability

Cysteine 46 of Histone lysine demethylase PHF8

Cysteine 70 of Histone lysine demethylase PHF8

A redox-regulated disulphide may form within Histone lysine demethylase PHF8 between cysteines 86 and 89 (50 and 53 respectively in this structure).

Details

Redox score ?
82
PDB code
3kv4
Structure name
structure of phf8 in complex with histone h3
Structure deposition date
2009-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
12
Peptide accession
Q9UPP1
Residue number A
86
Residue number B
89
Peptide name
Histone lysine demethylase PHF8

Ligandability

Cysteine 86 of Histone lysine demethylase PHF8

Cysteine 89 of Histone lysine demethylase PHF8

A redox-regulated disulphide may form within Histone lysine demethylase PHF8 between cysteines 62 and 86 (26 and 50 respectively in this structure).

Details

Redox score ?
82
PDB code
3kv4
Structure name
structure of phf8 in complex with histone h3
Structure deposition date
2009-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
18
Peptide accession
Q9UPP1
Residue number A
62
Residue number B
86
Peptide name
Histone lysine demethylase PHF8

Ligandability

Cysteine 62 of Histone lysine demethylase PHF8

Cysteine 86 of Histone lysine demethylase PHF8

A redox-regulated disulphide may form within Histone lysine demethylase PHF8 between cysteines 44 and 46 (8 and 10 respectively in this structure).

Details

Redox score ?
82
PDB code
3kv4
Structure name
structure of phf8 in complex with histone h3
Structure deposition date
2009-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
16
Peptide accession
Q9UPP1
Residue number A
44
Residue number B
46
Peptide name
Histone lysine demethylase PHF8

Ligandability

Cysteine 44 of Histone lysine demethylase PHF8

Cysteine 46 of Histone lysine demethylase PHF8

A redox-regulated disulphide may form within Histone lysine demethylase PHF8 between cysteines 59 and 89 (23 and 53 respectively in this structure).

Details

Redox score ?
80
PDB code
3kv4
Structure name
structure of phf8 in complex with histone h3
Structure deposition date
2009-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
16
Peptide accession
Q9UPP1
Residue number A
59
Residue number B
89
Peptide name
Histone lysine demethylase PHF8

Ligandability

Cysteine 59 of Histone lysine demethylase PHF8

Cysteine 89 of Histone lysine demethylase PHF8

A redox-regulated disulphide may form within Histone lysine demethylase PHF8 between cysteines 59 and 86 (23 and 50 respectively in this structure).

Details

Redox score ?
80
PDB code
3kv4
Structure name
structure of phf8 in complex with histone h3
Structure deposition date
2009-11-29
Thiol separation (Å)
3
Half-sphere exposure sum ?
68
Minimum pKa ?
8
% buried
28
Peptide accession
Q9UPP1
Residue number A
59
Residue number B
86
Peptide name
Histone lysine demethylase PHF8

Ligandability

Cysteine 59 of Histone lysine demethylase PHF8

Cysteine 86 of Histone lysine demethylase PHF8

A redox-regulated disulphide may form within Histone lysine demethylase PHF8 between cysteines 59 and 62 (23 and 26 respectively in this structure).

Details

Redox score ?
78
PDB code
3kv4
Structure name
structure of phf8 in complex with histone h3
Structure deposition date
2009-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
24
Peptide accession
Q9UPP1
Residue number A
59
Residue number B
62
Peptide name
Histone lysine demethylase PHF8

Ligandability

Cysteine 59 of Histone lysine demethylase PHF8

Cysteine 62 of Histone lysine demethylase PHF8

A redox-regulated disulphide may form within Histone lysine demethylase PHF8 between cysteines 44 and 86 (8 and 50 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3kv4
Structure name
structure of phf8 in complex with histone h3
Structure deposition date
2009-11-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
26
Peptide accession
Q9UPP1
Residue number A
44
Residue number B
86
Peptide name
Histone lysine demethylase PHF8

Ligandability

Cysteine 44 of Histone lysine demethylase PHF8

Cysteine 86 of Histone lysine demethylase PHF8

A redox-regulated disulphide may form within Histone lysine demethylase PHF8 between cysteines 271 and 363 (235 and 327 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
3k3o
Structure name
crystal structure of the catalytic core domain of human phf8 complexed with alpha-ketoglutarate
Structure deposition date
2009-10-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
98
Peptide accession
Q5JPR9
Residue number A
271
Residue number B
363
Peptide name
Histone lysine demethylase PHF8

Ligandability

Cysteine 271 of Histone lysine demethylase PHF8

Cysteine 363 of Histone lysine demethylase PHF8

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