ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Ras-associated and pleckstrin homology domains-containing protein 1

Intramolecular
Cysteine 467 and cysteine 486
Cysteine 486 and cysteine 487
Cysteine 388 and cysteine 390
Cysteine 467 and cysteine 487
A redox-regulated disulphide may form within Ras-associated and pleckstrin homology domains-containing protein 1 between cysteines 467 and 486.

Details

Redox score ?
72
PDB code
4gn1
Structure name
crystal structure of the ra and ph domains of lamellipodin
Structure deposition date
2012-08-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
88
Minimum pKa ?
7
% buried
68
Peptide accession
Q70E73
Residue number A
467
Residue number B
486
Peptide name
Ras-associated and pleckstrin homology domains-containing protein 1

Ligandability

Cysteine 467 of Ras-associated and pleckstrin homology domains-containing protein 1

Cysteine 486 of Ras-associated and pleckstrin homology domains-containing protein 1

A redox-regulated disulphide may form within Ras-associated and pleckstrin homology domains-containing protein 1 between cysteines 486 and 487. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
4gmv
Structure name
crystal structure of the coiled-coil, ra and ph domains of lamellipodin
Structure deposition date
2012-08-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
7
% buried
74
Peptide accession
Q70E73
Residue number A
486
Residue number B
487
Peptide name
Ras-associated and pleckstrin homology domains-containing protein 1

Ligandability

Cysteine 486 of Ras-associated and pleckstrin homology domains-containing protein 1

Cysteine 487 of Ras-associated and pleckstrin homology domains-containing protein 1

A redox-regulated disulphide may form within Ras-associated and pleckstrin homology domains-containing protein 1 between cysteines 388 and 390. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4gn1
Structure name
crystal structure of the ra and ph domains of lamellipodin
Structure deposition date
2012-08-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
34
Peptide accession
Q70E73
Residue number A
388
Residue number B
390
Peptide name
Ras-associated and pleckstrin homology domains-containing protein 1

Ligandability

Cysteine 388 of Ras-associated and pleckstrin homology domains-containing protein 1

Cysteine 390 of Ras-associated and pleckstrin homology domains-containing protein 1

A redox-regulated disulphide may form within Ras-associated and pleckstrin homology domains-containing protein 1 between cysteines 467 and 487. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4gmv
Structure name
crystal structure of the coiled-coil, ra and ph domains of lamellipodin
Structure deposition date
2012-08-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
13
% buried
82
Peptide accession
Q70E73
Residue number A
467
Residue number B
487
Peptide name
Ras-associated and pleckstrin homology domains-containing protein 1

Ligandability

Cysteine 467 of Ras-associated and pleckstrin homology domains-containing protein 1

Cysteine 487 of Ras-associated and pleckstrin homology domains-containing protein 1

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