ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Rho guanine nucleotide exchange factor 2

Intramolecular
Cysteine 67 and cysteine 307
Cysteine 282 and cysteine 342
A redox-regulated disulphide may form within Rho guanine nucleotide exchange factor 2 between cysteines 67 and 307 (67 and 104 respectively in this structure).

Details

Redox score ?
70
PDB code
5wi4
Structure name
crystal structure of dynlt1/tctex-1 in complex with arhgef2
Structure deposition date
2017-07-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
89
Minimum pKa ?
9
% buried
100
Peptide accession
Q60875
Residue number A
67
Residue number B
307
Peptide name
Rho guanine nucleotide exchange factor 2

Ligandability

Cysteine 67 of Rho guanine nucleotide exchange factor 2

Cysteine 307 of Rho guanine nucleotide exchange factor 2

Cysteine 67 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Rho guanine nucleotide exchange factor 2 between cysteines 282 and 342. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
8bnt
Structure name
the dh domain of arhgef2 bound to rhoa
Structure deposition date
2022-11-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
76
Peptide accession
Q92974
Residue number A
282
Residue number B
342
Peptide name
Rho guanine nucleotide exchange factor 2

Ligandability

Cysteine 282 of Rho guanine nucleotide exchange factor 2

Cysteine 342 of Rho guanine nucleotide exchange factor 2

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