ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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PDZ and LIM domain protein 1

Intramolecular
Cysteine 286 and cysteine 307
Cysteine 260 and cysteine 263
Cysteine 286 and cysteine 289
Cysteine 260 and cysteine 283
Cysteine 263 and cysteine 283
Cysteine 289 and cysteine 307
A redox-regulated disulphide may form within PDZ and LIM domain protein 1 between cysteines 286 and 307 (44 and 65 respectively in this structure).

Details

Redox score ?
88
PDB code
1x62
Structure name
solution structure of the lim domain of carboxyl terminal lim domain protein 1
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
5
% buried
6
Peptide accession
O00151
Residue number A
286
Residue number B
307
Peptide name
PDZ and LIM domain protein 1

Ligandability

Cysteine 286 of PDZ and LIM domain protein 1

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 307 of PDZ and LIM domain protein 1

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 PDZ and LIM domain protein 1 between cysteines 260 and 263 (18 and 21 respectively in this structure).

Details

Redox score ?
88
PDB code
1x62
Structure name
solution structure of the lim domain of carboxyl terminal lim domain protein 1
Structure deposition date
2005-05-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
40
Minimum pKa ?
6
% buried
8
Peptide accession
O00151
Residue number A
260
Residue number B
263
Peptide name
PDZ and LIM domain protein 1

Ligandability

Cysteine 260 of PDZ and LIM domain protein 1

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 263 of PDZ and LIM domain protein 1

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 PDZ and LIM domain protein 1 between cysteines 286 and 289 (44 and 47 respectively in this structure).

Details

Redox score ?
88
PDB code
1x62
Structure name
solution structure of the lim domain of carboxyl terminal lim domain protein 1
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
5
% buried
6
Peptide accession
O00151
Residue number A
286
Residue number B
289
Peptide name
PDZ and LIM domain protein 1

Ligandability

Cysteine 286 of PDZ and LIM domain protein 1

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 289 of PDZ and LIM domain protein 1

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 PDZ and LIM domain protein 1 between cysteines 260 and 283 (18 and 41 respectively in this structure).

Details

Redox score ?
84
PDB code
1x62
Structure name
solution structure of the lim domain of carboxyl terminal lim domain protein 1
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
12
Peptide accession
O00151
Residue number A
260
Residue number B
283
Peptide name
PDZ and LIM domain protein 1

Ligandability

Cysteine 260 of PDZ and LIM domain protein 1

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 283 of PDZ and LIM domain protein 1

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 PDZ and LIM domain protein 1 between cysteines 263 and 283 (21 and 41 respectively in this structure).

Details

Redox score ?
80
PDB code
1x62
Structure name
solution structure of the lim domain of carboxyl terminal lim domain protein 1
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
4
Peptide accession
O00151
Residue number A
263
Residue number B
283
Peptide name
PDZ and LIM domain protein 1

Ligandability

Cysteine 263 of PDZ and LIM domain protein 1

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 283 of PDZ and LIM domain protein 1

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 PDZ and LIM domain protein 1 between cysteines 289 and 307 (47 and 65 respectively in this structure).

Details

Redox score ?
79
PDB code
1x62
Structure name
solution structure of the lim domain of carboxyl terminal lim domain protein 1
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
0
Peptide accession
O00151
Residue number A
289
Residue number B
307
Peptide name
PDZ and LIM domain protein 1

Ligandability

Cysteine 289 of PDZ and LIM domain protein 1

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 307 of PDZ and LIM domain protein 1

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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