ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

UMP-CMP kinase

Intramolecular
Cysteine 122 and cysteine 127
Cysteine 127 and cysteine 131
Cysteine 122 and cysteine 131
A redox-regulated disulphide may form within UMP-CMP kinase between cysteines 122 and 127.

Details

Redox score ?
75
PDB code
7e9v
Structure name
the crystal structure of human ump-cmp kinase from biortus
Structure deposition date
2021-03-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
44
Peptide accession
P30085
Residue number A
122
Residue number B
127
Peptide name
UMP-CMP kinase

Ligandability

Cysteine 122 of UMP-CMP kinase

Cysteine 127 of UMP-CMP kinase

A redox-regulated disulphide may form within UMP-CMP kinase between cysteines 127 and 131. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
7e9v
Structure name
the crystal structure of human ump-cmp kinase from biortus
Structure deposition date
2021-03-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
38
Peptide accession
P30085
Residue number A
127
Residue number B
131
Peptide name
UMP-CMP kinase

Ligandability

Cysteine 127 of UMP-CMP kinase

Cysteine 131 of UMP-CMP kinase

A redox-regulated disulphide may form within UMP-CMP kinase between cysteines 122 and 131. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7e9v
Structure name
the crystal structure of human ump-cmp kinase from biortus
Structure deposition date
2021-03-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
33
Peptide accession
P30085
Residue number A
122
Residue number B
131
Peptide name
UMP-CMP kinase

Ligandability

Cysteine 122 of UMP-CMP kinase

Cysteine 131 of UMP-CMP kinase

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