ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein 692

Intramolecular
Cysteine 361 and cysteine 366
Cysteine 330 and cysteine 335
Cysteine 419 and cysteine 422
Cysteine 419 and cysteine 426
Cysteine 366 and cysteine 391
A redox-regulated disulphide may form within Zinc finger protein 692 between cysteines 361 and 366 (41 and 46 respectively in this structure).

Details

Redox score ?
87
PDB code
2dlk
Structure name
solution structure of the first and the second zf-c2h2 domains of zinc finger protein 692
Structure deposition date
2006-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
8
% buried
0
Peptide accession
Q9BU19
Residue number A
361
Residue number B
366
Peptide name
Zinc finger protein 692

Ligandability

Cysteine 361 of Zinc finger protein 692

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 366 of Zinc finger protein 692

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 692 between cysteines 330 and 335 (10 and 15 respectively in this structure).

Details

Redox score ?
86
PDB code
2dlk
Structure name
solution structure of the first and the second zf-c2h2 domains of zinc finger protein 692
Structure deposition date
2006-04-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
8
% buried
0
Peptide accession
Q9BU19
Residue number A
330
Residue number B
335
Peptide name
Zinc finger protein 692

Ligandability

Cysteine 330 of Zinc finger protein 692

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 335 of Zinc finger protein 692

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 692 between cysteines 419 and 422.

Details

Redox score ?
84
PDB code
6h0g
Structure name
structure of the ddb1-crbn-pomalidomide complex bound to znf692(zf4)
Structure deposition date
2018-07-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
65
Minimum pKa ?
2
% buried
73
Peptide accession
Q9BU19
Residue number A
419
Residue number B
422
Peptide name
Zinc finger protein 692

Ligandability

Cysteine 419 of Zinc finger protein 692

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 422 of Zinc finger protein 692

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 692 between cysteines 419 and 426.

Details

Redox score ?
66
PDB code
6h0g
Structure name
structure of the ddb1-crbn-pomalidomide complex bound to znf692(zf4)
Structure deposition date
2018-07-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
0
% buried
29
Peptide accession
Q9BU19
Residue number A
419
Residue number B
426
Peptide name
Zinc finger protein 692

Ligandability

Cysteine 419 of Zinc finger protein 692

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 426 of Zinc finger protein 692

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 692 between cysteines 366 and 391 (46 and 71 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
2dlk
Structure name
solution structure of the first and the second zf-c2h2 domains of zinc finger protein 692
Structure deposition date
2006-04-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
24
Minimum pKa ?
9
% buried
0
Peptide accession
Q9BU19
Residue number A
366
Residue number B
391
Peptide name
Zinc finger protein 692

Ligandability

Cysteine 366 of Zinc finger protein 692

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 391 of Zinc finger protein 692

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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