ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Ketimine reductase mu-crystallin

Intermolecular
Cysteine 283 and cysteine 283
Intramolecular
Cysteine 140 and cysteine 188
A redox-regulated disulphide may form between two units of Ketimine reductase mu-crystallin at cysteines 283 and 283.

Details

Redox score ?
75
PDB code
4bv8
Structure name
crystal structure of the apo form of mouse mu-crystallin
Structure deposition date
2013-06-25
Thiol separation (Å)
3
Half-sphere exposure sum ?
86
Minimum pKa ?
8
% buried
92
Peptide A name
Ketimine reductase mu-crystallin
Peptide B name
Ketimine reductase mu-crystallin
Peptide A accession
O54983
Peptide B accession
O54983
Peptide A residue number
283
Peptide B residue number
283

Ligandability

A redox-regulated disulphide may form within Ketimine reductase mu-crystallin between cysteines 140 and 188. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
2i99
Structure name
crystal structure of human mu_crystallin at 2
Structure deposition date
2006-09-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
70
Peptide accession
Q14894
Residue number A
140
Residue number B
188
Peptide name
Ketimine reductase mu-crystallin

Ligandability

Cysteine 140 of Ketimine reductase mu-crystallin

Cysteine 188 of Ketimine reductase mu-crystallin

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