ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein 568

Intramolecular
Cysteine 449 and cysteine 508
Cysteine 393 and cysteine 396
Cysteine 617 and cysteine 620
Cysteine 421 and cysteine 424
Cysteine 645 and cysteine 648
A redox-regulated disulphide may form within Zinc finger protein 568 between cysteines 449 and 508 (505 and 508 respectively in this structure).

Details

Redox score ?
93
PDB code
5v3j
Structure name
mousezfp568-znf1-10 in complex with dna
Structure deposition date
2017-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
4
% buried
0
Peptide accession
E9PYI1
Residue number A
449
Residue number B
508
Peptide name
Zinc finger protein 568

Ligandability

Cysteine 449 of Zinc finger protein 568

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 508 of Zinc finger protein 568

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 568 between cysteines 393 and 396.

Details

Redox score ?
88
PDB code
5wjq
Structure name
mousezfp568-znf2-11 in complex with dna
Structure deposition date
2017-07-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
6
% buried
0
Peptide accession
E9PYI1
Residue number A
393
Residue number B
396
Peptide name
Zinc finger protein 568

Ligandability

Cysteine 393 of Zinc finger protein 568

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 396 of Zinc finger protein 568

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 568 between cysteines 617 and 620.

Details

Redox score ?
84
PDB code
5v3m
Structure name
mousezfp568-znf1-11 in complex with dna
Structure deposition date
2017-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
8
% buried
nan
Peptide accession
E9PYI1
Residue number A
617
Residue number B
620
Peptide name
Zinc finger protein 568

Ligandability

Cysteine 617 of Zinc finger protein 568

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 620 of Zinc finger protein 568

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 568 between cysteines 421 and 424.

Details

Redox score ?
82
PDB code
5v3j
Structure name
mousezfp568-znf1-10 in complex with dna
Structure deposition date
2017-03-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
44
Peptide accession
E9PYI1
Residue number A
421
Residue number B
424
Peptide name
Zinc finger protein 568

Ligandability

Cysteine 421 of Zinc finger protein 568

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 424 of Zinc finger protein 568

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 568 between cysteines 645 and 648.

Details

Redox score ?
74
PDB code
5wjq
Structure name
mousezfp568-znf2-11 in complex with dna
Structure deposition date
2017-07-24
Thiol separation (Å)
5
Half-sphere exposure sum ?
35
Minimum pKa ?
8
% buried
0
Peptide accession
E9PYI1
Residue number A
645
Residue number B
648
Peptide name
Zinc finger protein 568

Ligandability

Cysteine 645 of Zinc finger protein 568

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 648 of Zinc finger protein 568

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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