ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein ZFPM1

Intramolecular
Cysteine 335 and cysteine 338
Cysteine 335 and cysteine 348
Cysteine 338 and cysteine 348
Cysteine 161 and cysteine 188
A redox-regulated disulphide may form within Zinc finger protein ZFPM1 between cysteines 335 and 338 (10 and 13 respectively in this structure).

Details

Redox score ?
89
PDB code
1srk
Structure name
solution structure of the third zinc finger domain of fog-1
Structure deposition date
2004-03-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
6
% buried
0
Peptide accession
O35615
Residue number A
335
Residue number B
338
Peptide name
Zinc finger protein ZFPM1

Ligandability

Cysteine 335 of Zinc finger protein ZFPM1

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 338 of Zinc finger protein ZFPM1

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 ZFPM1 between cysteines 335 and 348 (10 and 23 respectively in this structure).

Details

Redox score ?
76
PDB code
1srk
Structure name
solution structure of the third zinc finger domain of fog-1
Structure deposition date
2004-03-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
0
Peptide accession
O35615
Residue number A
335
Residue number B
348
Peptide name
Zinc finger protein ZFPM1

Ligandability

Cysteine 335 of Zinc finger protein ZFPM1

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 348 of Zinc finger protein ZFPM1

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 ZFPM1 between cysteines 338 and 348 (13 and 23 respectively in this structure).

Details

Redox score ?
62
PDB code
1srk
Structure name
solution structure of the third zinc finger domain of fog-1
Structure deposition date
2004-03-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
43
Minimum pKa ?
6
% buried
0
Peptide accession
O35615
Residue number A
338
Residue number B
348
Peptide name
Zinc finger protein ZFPM1

Ligandability

Cysteine 338 of Zinc finger protein ZFPM1

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 348 of Zinc finger protein ZFPM1

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 ZFPM1 between cysteines 161 and 188. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2mpl
Structure name
solution structure of the pr domain of fog-1
Structure deposition date
2014-05-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
68
Peptide accession
O35615
Residue number A
161
Residue number B
188
Peptide name
Zinc finger protein ZFPM1

Ligandability

Cysteine 161 of Zinc finger protein ZFPM1

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 188 of Zinc finger protein ZFPM1

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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