ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein 32

Intramolecular
Cysteine 247 and cysteine 250
Cysteine 247 and cysteine 267
Cysteine 79 and cysteine 82
Cysteine 107 and cysteine 110
Cysteine 250 and cysteine 267
A redox-regulated disulphide may form within Zinc finger protein 32 between cysteines 247 and 250.

Details

Redox score ?
90
PDB code
2epc
Structure name
solution structure of zinc finger domain 7 in zinc finger protein 32
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
6
% buried
0
Peptide accession
P17041
Residue number A
247
Residue number B
250
Peptide name
Zinc finger protein 32

Ligandability

Cysteine 247 of Zinc finger protein 32

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 250 of Zinc finger protein 32

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 Zinc finger protein 32 between cysteines 247 and 267.

Details

Redox score ?
90
PDB code
2epc
Structure name
solution structure of zinc finger domain 7 in zinc finger protein 32
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
6
% buried
0
Peptide accession
P17041
Residue number A
247
Residue number B
267
Peptide name
Zinc finger protein 32

Ligandability

Cysteine 247 of Zinc finger protein 32

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 267 of Zinc finger protein 32

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 Zinc finger protein 32 between cysteines 79 and 82.

Details

Redox score ?
87
PDB code
2ept
Structure name
solution structure of the first c2h2 type zinc finger domain of zinc finger protein 32
Structure deposition date
2007-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
7
% buried
0
Peptide accession
P17041
Residue number A
79
Residue number B
82
Peptide name
Zinc finger protein 32

Ligandability

Cysteine 79 of Zinc finger protein 32

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 82 of Zinc finger protein 32

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 Zinc finger protein 32 between cysteines 107 and 110.

Details

Redox score ?
84
PDB code
2epu
Structure name
solution structure of the secound c2h2 type zinc finger domain of zinc finger protein 32
Structure deposition date
2007-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
7
% buried
0
Peptide accession
P17041
Residue number A
107
Residue number B
110
Peptide name
Zinc finger protein 32

Ligandability

Cysteine 107 of Zinc finger protein 32

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 110 of Zinc finger protein 32

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 Zinc finger protein 32 between cysteines 250 and 267.

Details

Redox score ?
83
PDB code
2epc
Structure name
solution structure of zinc finger domain 7 in zinc finger protein 32
Structure deposition date
2007-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
33
Minimum pKa ?
8
% buried
0
Peptide accession
P17041
Residue number A
250
Residue number B
267
Peptide name
Zinc finger protein 32

Ligandability

Cysteine 250 of Zinc finger protein 32

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 267 of Zinc finger protein 32

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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