ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

General vesicular transport factor p115

Intramolecular
Cysteine 383 and cysteine 439 L
Cysteine 388 and cysteine 391 L
Cysteine 317 and cysteine 388
Cysteine 426 and cysteine 478
Cysteine 499 and cysteine 541
A redox-regulated disulphide may form within General vesicular transport factor p115 between cysteines 383 and 439. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3gq2
Structure name
crystal structure of the dimer of the p115 tether globular head domain
Structure deposition date
2009-03-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
91
Peptide accession
P41541
Residue number A
383
Residue number B
439
Peptide name
General vesicular transport factor p115

Ligandability

Cysteine 383 of General vesicular transport factor p115

Cysteine 439 of General vesicular transport factor p115

A redox-regulated disulphide may form within General vesicular transport factor p115 between cysteines 388 and 391. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2w3c
Structure name
globular head region of the human general vesicular transport factor p115
Structure deposition date
2008-11-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
O60763
Residue number A
388
Residue number B
391
Peptide name
General vesicular transport factor p115

Ligandability

Cysteine 388 of General vesicular transport factor p115

Cysteine 391 of General vesicular transport factor p115

A redox-regulated disulphide may form within General vesicular transport factor p115 between cysteines 317 and 388. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2w3c
Structure name
globular head region of the human general vesicular transport factor p115
Structure deposition date
2008-11-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
96
Peptide accession
O60763
Residue number A
317
Residue number B
388
Peptide name
General vesicular transport factor p115

Ligandability

Cysteine 317 of General vesicular transport factor p115

Cysteine 388 of General vesicular transport factor p115

A redox-regulated disulphide may form within General vesicular transport factor p115 between cysteines 426 and 478. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2w3c
Structure name
globular head region of the human general vesicular transport factor p115
Structure deposition date
2008-11-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
85
Peptide accession
O60763
Residue number A
426
Residue number B
478
Peptide name
General vesicular transport factor p115

Ligandability

Cysteine 426 of General vesicular transport factor p115

Cysteine 478 of General vesicular transport factor p115

A redox-regulated disulphide may form within General vesicular transport factor p115 between cysteines 499 and 541. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2w3c
Structure name
globular head region of the human general vesicular transport factor p115
Structure deposition date
2008-11-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
100
Peptide accession
O60763
Residue number A
499
Residue number B
541
Peptide name
General vesicular transport factor p115

Ligandability

Cysteine 499 of General vesicular transport factor p115

Cysteine 541 of General vesicular transport factor p115

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