ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Syntaxin-1A

Intermolecular
Cysteine 103 of Vesicle-associated membrane protein 2 and cysteine 271
Cysteine 103 of Vesicle-associated membrane protein 2 and cysteine 272
Intramolecular
Cysteine 271 and cysteine 272
A redox-regulated disulphide may form between cysteine 103 of Vesicle-associated membrane protein 2 and cysteine 271 of Syntaxin-1A.

Details

Redox score ?
76
PDB code
3hd7
Structure name
helical extension of the neuronal snare complex into the membrane, spacegroup c 1 2 1
Structure deposition date
2009-05-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
14
Peptide A name
Vesicle-associated membrane protein 2
Peptide B name
Syntaxin-1A
Peptide A accession
P63045
Peptide B accession
P32851
Peptide A residue number
103
Peptide B residue number
271

Ligandability

Cysteine 103 of Vesicle-associated membrane protein 2

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 271 of Syntaxin-1A

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 between cysteine 103 of Vesicle-associated membrane protein 2 and cysteine 272 of Syntaxin-1A. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3hd7
Structure name
helical extension of the neuronal snare complex into the membrane, spacegroup c 1 2 1
Structure deposition date
2009-05-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
24
Peptide A name
Vesicle-associated membrane protein 2
Peptide B name
Syntaxin-1A
Peptide A accession
P63045
Peptide B accession
P32851
Peptide A residue number
103
Peptide B residue number
272

Ligandability

Cysteine 103 of Vesicle-associated membrane protein 2

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 272 of Syntaxin-1A

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 Syntaxin-1A between cysteines 271 and 272. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
3hd7
Structure name
helical extension of the neuronal snare complex into the membrane, spacegroup c 1 2 1
Structure deposition date
2009-05-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
28
Peptide accession
P32851
Residue number A
271
Residue number B
272
Peptide name
Syntaxin-1A

Ligandability

Cysteine 271 of Syntaxin-1A

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 272 of Syntaxin-1A

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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