ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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PDZ and LIM domain protein 3

Intramolecular
Cysteine 272 and cysteine 275
Cysteine 246 and cysteine 249
Cysteine 246 and cysteine 269
Cysteine 272 and cysteine 293
Cysteine 275 and cysteine 293
Cysteine 249 and cysteine 269
A redox-regulated disulphide may form within PDZ and LIM domain protein 3 between cysteines 272 and 275 (54 and 57 respectively in this structure).

Details

Redox score ?
90
PDB code
1x64
Structure name
solution structure of the lim domain of alpha-actinin-2 associated lim protein
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
4
% buried
4
Peptide accession
O70209
Residue number A
272
Residue number B
275
Peptide name
PDZ and LIM domain protein 3

Ligandability

Cysteine 272 of PDZ and LIM domain 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 275 of PDZ and LIM domain 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 PDZ and LIM domain protein 3 between cysteines 246 and 249 (28 and 31 respectively in this structure).

Details

Redox score ?
89
PDB code
1x64
Structure name
solution structure of the lim domain of alpha-actinin-2 associated lim protein
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
5
% buried
3
Peptide accession
O70209
Residue number A
246
Residue number B
249
Peptide name
PDZ and LIM domain protein 3

Ligandability

Cysteine 246 of PDZ and LIM domain 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 249 of PDZ and LIM domain 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 PDZ and LIM domain protein 3 between cysteines 246 and 269 (28 and 51 respectively in this structure).

Details

Redox score ?
88
PDB code
1x64
Structure name
solution structure of the lim domain of alpha-actinin-2 associated lim protein
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
3
Peptide accession
O70209
Residue number A
246
Residue number B
269
Peptide name
PDZ and LIM domain protein 3

Ligandability

Cysteine 246 of PDZ and LIM domain 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 269 of PDZ and LIM domain 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 PDZ and LIM domain protein 3 between cysteines 272 and 293 (54 and 75 respectively in this structure).

Details

Redox score ?
88
PDB code
1x64
Structure name
solution structure of the lim domain of alpha-actinin-2 associated lim protein
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
4
% buried
5
Peptide accession
O70209
Residue number A
272
Residue number B
293
Peptide name
PDZ and LIM domain protein 3

Ligandability

Cysteine 272 of PDZ and LIM domain 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 293 of PDZ and LIM domain 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 PDZ and LIM domain protein 3 between cysteines 275 and 293 (57 and 75 respectively in this structure).

Details

Redox score ?
82
PDB code
1x64
Structure name
solution structure of the lim domain of alpha-actinin-2 associated lim protein
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
0
Peptide accession
O70209
Residue number A
275
Residue number B
293
Peptide name
PDZ and LIM domain protein 3

Ligandability

Cysteine 275 of PDZ and LIM domain 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 293 of PDZ and LIM domain 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 PDZ and LIM domain protein 3 between cysteines 249 and 269 (31 and 51 respectively in this structure).

Details

Redox score ?
78
PDB code
1x64
Structure name
solution structure of the lim domain of alpha-actinin-2 associated lim protein
Structure deposition date
2005-05-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
0
Peptide accession
O70209
Residue number A
249
Residue number B
269
Peptide name
PDZ and LIM domain protein 3

Ligandability

Cysteine 249 of PDZ and LIM domain 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 269 of PDZ and LIM domain 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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