ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger CCCH domain-containing protein 4

Intramolecular
Cysteine 425 and cysteine 439
Cysteine 457 and cysteine 463
Cysteine 425 and cysteine 433
Cysteine 448 and cysteine 457
Cysteine 433 and cysteine 439
Cysteine 448 and cysteine 463
A redox-regulated disulphide may form within Zinc finger CCCH domain-containing protein 4 between cysteines 425 and 439 (437 and 451 respectively in this structure).

Details

Redox score ?
93
PDB code
2cqe
Structure name
solution structure of the zinc-finger domain in kiaa1064 protein
Structure deposition date
2005-05-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
5
% buried
0
Peptide accession
Q9UPT8
Residue number A
425
Residue number B
439
Peptide name
Zinc finger CCCH domain-containing protein 4

Ligandability

Cysteine 425 of Zinc finger CCCH domain-containing protein 4

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 439 of Zinc finger CCCH domain-containing protein 4

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 CCCH domain-containing protein 4 between cysteines 457 and 463 (469 and 475 respectively in this structure).

Details

Redox score ?
92
PDB code
2cqe
Structure name
solution structure of the zinc-finger domain in kiaa1064 protein
Structure deposition date
2005-05-19
Thiol separation (Å)
3
Half-sphere exposure sum ?
39
Minimum pKa ?
7
% buried
0
Peptide accession
Q9UPT8
Residue number A
457
Residue number B
463
Peptide name
Zinc finger CCCH domain-containing protein 4

Ligandability

Cysteine 457 of Zinc finger CCCH domain-containing protein 4

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 463 of Zinc finger CCCH domain-containing protein 4

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 CCCH domain-containing protein 4 between cysteines 425 and 433 (437 and 445 respectively in this structure).

Details

Redox score ?
92
PDB code
2cqe
Structure name
solution structure of the zinc-finger domain in kiaa1064 protein
Structure deposition date
2005-05-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
5
% buried
0
Peptide accession
Q9UPT8
Residue number A
425
Residue number B
433
Peptide name
Zinc finger CCCH domain-containing protein 4

Ligandability

Cysteine 425 of Zinc finger CCCH domain-containing protein 4

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 433 of Zinc finger CCCH domain-containing protein 4

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 CCCH domain-containing protein 4 between cysteines 448 and 457 (460 and 469 respectively in this structure).

Details

Redox score ?
85
PDB code
2cqe
Structure name
solution structure of the zinc-finger domain in kiaa1064 protein
Structure deposition date
2005-05-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
7
Peptide accession
Q9UPT8
Residue number A
448
Residue number B
457
Peptide name
Zinc finger CCCH domain-containing protein 4

Ligandability

Cysteine 448 of Zinc finger CCCH domain-containing protein 4

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 457 of Zinc finger CCCH domain-containing protein 4

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 CCCH domain-containing protein 4 between cysteines 433 and 439 (445 and 451 respectively in this structure).

Details

Redox score ?
85
PDB code
2cqe
Structure name
solution structure of the zinc-finger domain in kiaa1064 protein
Structure deposition date
2005-05-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
9
% buried
0
Peptide accession
Q9UPT8
Residue number A
433
Residue number B
439
Peptide name
Zinc finger CCCH domain-containing protein 4

Ligandability

Cysteine 433 of Zinc finger CCCH domain-containing protein 4

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 439 of Zinc finger CCCH domain-containing protein 4

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 CCCH domain-containing protein 4 between cysteines 448 and 463 (460 and 475 respectively in this structure).

Details

Redox score ?
81
PDB code
2cqe
Structure name
solution structure of the zinc-finger domain in kiaa1064 protein
Structure deposition date
2005-05-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
7
Peptide accession
Q9UPT8
Residue number A
448
Residue number B
463
Peptide name
Zinc finger CCCH domain-containing protein 4

Ligandability

Cysteine 448 of Zinc finger CCCH domain-containing protein 4

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 463 of Zinc finger CCCH domain-containing protein 4

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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