ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein diaphanous homolog 1

Intermolecular
Cysteine 428 and cysteine 428
Intramolecular
Cysteine 155 and cysteine 211
Cysteine 428 and cysteine 445
A redox-regulated disulphide may form between two units of Protein diaphanous homolog 1 at cysteines 428 and 428.

Details

Redox score ?
67
PDB code
3obv
Structure name
autoinhibited formin mdia1 structure
Structure deposition date
2010-08-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
100
Peptide A name
Protein diaphanous homolog 1
Peptide B name
Protein diaphanous homolog 1
Peptide A accession
O08808
Peptide B accession
O08808
Peptide A residue number
428
Peptide B residue number
428

Ligandability

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 Protein diaphanous homolog 1 between cysteines 155 and 211. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3o4x
Structure name
crystal structure of complex between amino and carboxy terminal fragments of mdia1
Structure deposition date
2010-07-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
70
Peptide accession
O08808
Residue number A
155
Residue number B
211
Peptide name
Protein diaphanous homolog 1

Ligandability

Cysteine 155 of Protein diaphanous homolog 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 211 of Protein diaphanous homolog 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 Protein diaphanous homolog 1 between cysteines 428 and 445. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
2bnx
Structure name
crystal structure of the dimeric regulatory domain of mouse diaphaneous-related formin (drf), mdia1
Structure deposition date
2005-04-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
14
% buried
100
Peptide accession
O08808
Residue number A
428
Residue number B
445
Peptide name
Protein diaphanous homolog 1

Ligandability

Cysteine 428 of Protein diaphanous homolog 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 445 of Protein diaphanous homolog 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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