ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

RAC-alpha serine/threonine-protein kinase

Intramolecular
Cysteine 60 and cysteine 77
Cysteine 296 and cysteine 310
A redox-regulated disulphide may form within RAC-alpha serine/threonine-protein kinase between cysteines 60 and 77. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
1h10
Structure name
high resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to ins(1,3,4,5)-tetrakisphophate
Structure deposition date
2002-07-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
11
% buried
58
Peptide accession
P31749
Residue number A
60
Residue number B
77
Peptide name
RAC-alpha serine/threonine-protein kinase

Ligandability

Cysteine 60 of RAC-alpha serine/threonine-protein kinase

Cysteine 77 of RAC-alpha serine/threonine-protein kinase

A redox-regulated disulphide may form within RAC-alpha serine/threonine-protein kinase between cysteines 296 and 310. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
3ocb
Structure name
akt1 kinase domain with pyrrolopyrimidine inhibitor
Structure deposition date
2010-08-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
90
Peptide accession
B2RAM5
Residue number A
296
Residue number B
310
Peptide name
RAC-alpha serine/threonine-protein kinase

Ligandability

Cysteine 296 of RAC-alpha serine/threonine-protein kinase

Cysteine 310 of RAC-alpha serine/threonine-protein kinase

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