ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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AN1-type zinc finger protein 3

Intramolecular
Cysteine 157 and cysteine 160
Cysteine 174 and cysteine 192
Cysteine 174 and cysteine 176
Cysteine 176 and cysteine 192
Cysteine 157 and cysteine 181
Cysteine 160 and cysteine 181
A redox-regulated disulphide may form within AN1-type zinc finger protein 3 between cysteines 157 and 160 (18 and 21 respectively in this structure).

Details

Redox score ?
86
PDB code
1x4w
Structure name
solution structure of the zf-an1 domain from human hypothetical protein flj13222
Structure deposition date
2005-05-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
5
% buried
14
Peptide accession
Q9H8U3
Residue number A
157
Residue number B
160
Peptide name
AN1-type zinc finger protein 3

Ligandability

Cysteine 157 of AN1-type zinc finger protein 3

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 160 of AN1-type zinc finger protein 3

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 AN1-type zinc finger protein 3 between cysteines 174 and 192 (35 and 53 respectively in this structure).

Details

Redox score ?
86
PDB code
1x4w
Structure name
solution structure of the zf-an1 domain from human hypothetical protein flj13222
Structure deposition date
2005-05-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
7
% buried
6
Peptide accession
Q9H8U3
Residue number A
174
Residue number B
192
Peptide name
AN1-type zinc finger protein 3

Ligandability

Cysteine 174 of AN1-type zinc finger protein 3

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 192 of AN1-type zinc finger protein 3

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 AN1-type zinc finger protein 3 between cysteines 174 and 176 (35 and 37 respectively in this structure).

Details

Redox score ?
84
PDB code
1x4w
Structure name
solution structure of the zf-an1 domain from human hypothetical protein flj13222
Structure deposition date
2005-05-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
7
% buried
13
Peptide accession
Q9H8U3
Residue number A
174
Residue number B
176
Peptide name
AN1-type zinc finger protein 3

Ligandability

Cysteine 174 of AN1-type zinc finger protein 3

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 176 of AN1-type zinc finger protein 3

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 AN1-type zinc finger protein 3 between cysteines 176 and 192 (37 and 53 respectively in this structure).

Details

Redox score ?
84
PDB code
1x4w
Structure name
solution structure of the zf-an1 domain from human hypothetical protein flj13222
Structure deposition date
2005-05-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
9
% buried
6
Peptide accession
Q9H8U3
Residue number A
176
Residue number B
192
Peptide name
AN1-type zinc finger protein 3

Ligandability

Cysteine 176 of AN1-type zinc finger protein 3

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 192 of AN1-type zinc finger protein 3

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 AN1-type zinc finger protein 3 between cysteines 157 and 181 (18 and 42 respectively in this structure).

Details

Redox score ?
84
PDB code
1x4w
Structure name
solution structure of the zf-an1 domain from human hypothetical protein flj13222
Structure deposition date
2005-05-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
5
% buried
16
Peptide accession
Q9H8U3
Residue number A
157
Residue number B
181
Peptide name
AN1-type zinc finger protein 3

Ligandability

Cysteine 157 of AN1-type zinc finger protein 3

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 181 of AN1-type zinc finger protein 3

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 AN1-type zinc finger protein 3 between cysteines 160 and 181 (21 and 42 respectively in this structure).

Details

Redox score ?
77
PDB code
1x4w
Structure name
solution structure of the zf-an1 domain from human hypothetical protein flj13222
Structure deposition date
2005-05-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
8
Peptide accession
Q9H8U3
Residue number A
160
Residue number B
181
Peptide name
AN1-type zinc finger protein 3

Ligandability

Cysteine 160 of AN1-type zinc finger protein 3

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 181 of AN1-type zinc finger protein 3

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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