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Lysine-specific demethylase PHF2

Intramolecular
Cysteine 23 and cysteine 53
Cysteine 23 and cysteine 26
Cysteine 50 and cysteine 53
Cysteine 23 and cysteine 50
Cysteine 8 and cysteine 34
Cysteine 26 and cysteine 53
Cysteine 26 and cysteine 50
Cysteine 10 and cysteine 34
Cysteine 8 and cysteine 10
Cysteine 240 and cysteine 329
More...
Cysteine 8 and cysteine 50
Cysteine 237 and cysteine 240
Cysteine 237 and cysteine 329
A redox-regulated disulphide may form within Lysine-specific demethylase PHF2 between cysteines 23 and 53.

Details

Redox score ?
87
PDB code
8f8z
Structure name
phf2 (phd+jmj) in complex with h3 histone n-terminal peptide
Structure deposition date
2022-11-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
15
Peptide accession
O75151
Residue number A
23
Residue number B
53
Peptide name
Lysine-specific demethylase PHF2

Ligandability

Cysteine 23 of Lysine-specific demethylase PHF2

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 53 of Lysine-specific demethylase PHF2

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 PHF2 between cysteines 23 and 26.

Details

Redox score ?
84
PDB code
8f8z
Structure name
phf2 (phd+jmj) in complex with h3 histone n-terminal peptide
Structure deposition date
2022-11-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
28
Peptide accession
O75151
Residue number A
23
Residue number B
26
Peptide name
Lysine-specific demethylase PHF2

Ligandability

Cysteine 23 of Lysine-specific demethylase PHF2

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 26 of Lysine-specific demethylase PHF2

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 PHF2 between cysteines 50 and 53.

Details

Redox score ?
83
PDB code
8f8z
Structure name
phf2 (phd+jmj) in complex with h3 histone n-terminal peptide
Structure deposition date
2022-11-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
10
Peptide accession
O75151
Residue number A
50
Residue number B
53
Peptide name
Lysine-specific demethylase PHF2

Ligandability

Cysteine 50 of Lysine-specific demethylase PHF2

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 53 of Lysine-specific demethylase PHF2

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 PHF2 between cysteines 23 and 50.

Details

Redox score ?
83
PDB code
8f8z
Structure name
phf2 (phd+jmj) in complex with h3 histone n-terminal peptide
Structure deposition date
2022-11-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
6
% buried
24
Peptide accession
O75151
Residue number A
23
Residue number B
50
Peptide name
Lysine-specific demethylase PHF2

Ligandability

Cysteine 23 of Lysine-specific demethylase PHF2

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 50 of Lysine-specific demethylase PHF2

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 PHF2 between cysteines 8 and 34.

Details

Redox score ?
80
PDB code
8f8z
Structure name
phf2 (phd+jmj) in complex with h3 histone n-terminal peptide
Structure deposition date
2022-11-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
nan
Peptide accession
O75151
Residue number A
8
Residue number B
34
Peptide name
Lysine-specific demethylase PHF2

Ligandability

Cysteine 8 of Lysine-specific demethylase PHF2

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 34 of Lysine-specific demethylase PHF2

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 PHF2 between cysteines 26 and 53.

Details

Redox score ?
78
PDB code
8f8z
Structure name
phf2 (phd+jmj) in complex with h3 histone n-terminal peptide
Structure deposition date
2022-11-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
10
% buried
12
Peptide accession
O75151
Residue number A
26
Residue number B
53
Peptide name
Lysine-specific demethylase PHF2

Ligandability

Cysteine 26 of Lysine-specific demethylase PHF2

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 53 of Lysine-specific demethylase PHF2

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 PHF2 between cysteines 26 and 50.

Details

Redox score ?
77
PDB code
8f8z
Structure name
phf2 (phd+jmj) in complex with h3 histone n-terminal peptide
Structure deposition date
2022-11-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
22
Peptide accession
O75151
Residue number A
26
Residue number B
50
Peptide name
Lysine-specific demethylase PHF2

Ligandability

Cysteine 26 of Lysine-specific demethylase PHF2

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 50 of Lysine-specific demethylase PHF2

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 PHF2 between cysteines 10 and 34.

Details

Redox score ?
74
PDB code
8f8y
Structure name
phf2 (phd+jmj) in complex with vrk1 n-terminal peptide
Structure deposition date
2022-11-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
56
Peptide accession
O75151
Residue number A
10
Residue number B
34
Peptide name
Lysine-specific demethylase PHF2

Ligandability

Cysteine 10 of Lysine-specific demethylase PHF2

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 34 of Lysine-specific demethylase PHF2

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 PHF2 between cysteines 8 and 10.

Details

Redox score ?
62
PDB code
8f8z
Structure name
phf2 (phd+jmj) in complex with h3 histone n-terminal peptide
Structure deposition date
2022-11-22
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
18
% buried
nan
Peptide accession
O75151
Residue number A
8
Residue number B
10
Peptide name
Lysine-specific demethylase PHF2

Ligandability

Cysteine 8 of Lysine-specific demethylase PHF2

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 10 of Lysine-specific demethylase PHF2

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 PHF2 between cysteines 240 and 329.

Details

Redox score ?
61
PDB code
8f8z
Structure name
phf2 (phd+jmj) in complex with h3 histone n-terminal peptide
Structure deposition date
2022-11-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
100
Peptide accession
O75151
Residue number A
240
Residue number B
329
Peptide name
Lysine-specific demethylase PHF2

Ligandability

Cysteine 240 of Lysine-specific demethylase PHF2

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 329 of Lysine-specific demethylase PHF2

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 PHF2 between cysteines 8 and 50. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
8f8y
Structure name
phf2 (phd+jmj) in complex with vrk1 n-terminal peptide
Structure deposition date
2022-11-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
nan
Peptide accession
O75151
Residue number A
8
Residue number B
50
Peptide name
Lysine-specific demethylase PHF2

Ligandability

Cysteine 8 of Lysine-specific demethylase PHF2

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 50 of Lysine-specific demethylase PHF2

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 PHF2 between cysteines 237 and 240. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
8f8z
Structure name
phf2 (phd+jmj) in complex with h3 histone n-terminal peptide
Structure deposition date
2022-11-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
9
% buried
100
Peptide accession
O75151
Residue number A
237
Residue number B
240
Peptide name
Lysine-specific demethylase PHF2

Ligandability

Cysteine 237 of Lysine-specific demethylase PHF2

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 240 of Lysine-specific demethylase PHF2

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 PHF2 between cysteines 237 and 329. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
8f8z
Structure name
phf2 (phd+jmj) in complex with h3 histone n-terminal peptide
Structure deposition date
2022-11-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
99
Peptide accession
O75151
Residue number A
237
Residue number B
329
Peptide name
Lysine-specific demethylase PHF2

Ligandability

Cysteine 237 of Lysine-specific demethylase PHF2

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 329 of Lysine-specific demethylase PHF2

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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