ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

NADH-cytochrome b5 reductase 3

Intramolecular
Cysteine 245 and cysteine 255
Cysteine 245 and cysteine 269
Cysteine 284 and cysteine 298
A redox-regulated disulphide may form within NADH-cytochrome b5 reductase 3 between cysteines 245 and 255.

Details

Redox score ?
87
PDB code
1ndh
Structure name
crystal structure of nadh-cytochrome b5 reductase from pig liver at 2
Structure deposition date
1994-10-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
72
Minimum pKa ?
3
% buried
62
Peptide accession
P83686
Residue number A
245
Residue number B
255
Peptide name
NADH-cytochrome b5 reductase 3

Ligandability

Cysteine 245 of NADH-cytochrome b5 reductase 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 255 of NADH-cytochrome b5 reductase 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within NADH-cytochrome b5 reductase 3 between cysteines 245 and 269. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
1ndh
Structure name
crystal structure of nadh-cytochrome b5 reductase from pig liver at 2
Structure deposition date
1994-10-31
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
15
% buried
70
Peptide accession
P83686
Residue number A
245
Residue number B
269
Peptide name
NADH-cytochrome b5 reductase 3

Ligandability

Cysteine 245 of NADH-cytochrome b5 reductase 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 269 of NADH-cytochrome b5 reductase 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within NADH-cytochrome b5 reductase 3 between cysteines 284 and 298. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
7tsw
Structure name
crystal structure of human nadh-cytochrome b5 reductase t117d mutant
Structure deposition date
2022-01-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
72
Peptide accession
P00387
Residue number A
284
Residue number B
298
Peptide name
NADH-cytochrome b5 reductase 3

Ligandability

Cysteine 284 of NADH-cytochrome b5 reductase 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 298 of NADH-cytochrome b5 reductase 3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

If this tool was useful for finding a disulphide, please cite: