ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein 512B

Intramolecular
Cysteine 512 and cysteine 533
Cysteine 542 and cysteine 545
Cysteine 512 and cysteine 515
Cysteine 515 and cysteine 533
A redox-regulated disulphide may form within Zinc finger protein 512B between cysteines 512 and 533 (27 and 48 respectively in this structure).

Details

Redox score ?
89
PDB code
2gqj
Structure name
solution structure of the two zf-c2h2 like domains(493-575) of human zinc finger protein kiaa1196
Structure deposition date
2006-04-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
4
Peptide accession
Q96KM6
Residue number A
512
Residue number B
533
Peptide name
Zinc finger protein 512B

Ligandability

Cysteine 512 of Zinc finger protein 512B

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 533 of Zinc finger protein 512B

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 512B between cysteines 542 and 545 (57 and 60 respectively in this structure).

Details

Redox score ?
89
PDB code
2gqj
Structure name
solution structure of the two zf-c2h2 like domains(493-575) of human zinc finger protein kiaa1196
Structure deposition date
2006-04-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
6
% buried
0
Peptide accession
Q96KM6
Residue number A
542
Residue number B
545
Peptide name
Zinc finger protein 512B

Ligandability

Cysteine 542 of Zinc finger protein 512B

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 545 of Zinc finger protein 512B

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 512B between cysteines 512 and 515 (27 and 30 respectively in this structure).

Details

Redox score ?
88
PDB code
2gqj
Structure name
solution structure of the two zf-c2h2 like domains(493-575) of human zinc finger protein kiaa1196
Structure deposition date
2006-04-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
4
Peptide accession
Q96KM6
Residue number A
512
Residue number B
515
Peptide name
Zinc finger protein 512B

Ligandability

Cysteine 512 of Zinc finger protein 512B

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 515 of Zinc finger protein 512B

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 512B between cysteines 515 and 533 (30 and 48 respectively in this structure).

Details

Redox score ?
80
PDB code
2gqj
Structure name
solution structure of the two zf-c2h2 like domains(493-575) of human zinc finger protein kiaa1196
Structure deposition date
2006-04-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
1
Peptide accession
Q96KM6
Residue number A
515
Residue number B
533
Peptide name
Zinc finger protein 512B

Ligandability

Cysteine 515 of Zinc finger protein 512B

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 533 of Zinc finger protein 512B

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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