ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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NADPH--cytochrome P450 reductase

Intramolecular
Cysteine 363 and cysteine 445
Cysteine 472 and cysteine 629
Cysteine 147 and cysteine 363
A redox-regulated disulphide may form within NADPH--cytochrome P450 reductase between cysteines 363 and 445 (366 and 448 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3qe2
Structure name
crystal structure of human nadph-cytochrome p450 reductase
Structure deposition date
2011-01-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
88
Peptide accession
P16435
Residue number A
363
Residue number B
445
Peptide name
NADPH--cytochrome P450 reductase

Ligandability

Cysteine 363 of NADPH--cytochrome P450 reductase

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 445 of NADPH--cytochrome P450 reductase

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 NADPH--cytochrome P450 reductase between cysteines 472 and 629 (475 and 632 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
3qfr
Structure name
crystal structure of human nadph-cytochrome p450 reductase (r457h mutant)
Structure deposition date
2011-01-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
P16435
Residue number A
472
Residue number B
629
Peptide name
NADPH--cytochrome P450 reductase

Ligandability

Cysteine 472 of NADPH--cytochrome P450 reductase

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 629 of NADPH--cytochrome P450 reductase

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 NADPH--cytochrome P450 reductase between cysteines 147 and 363 (147 and 514 respectively in this structure).

Details

Redox score ?
nan
PDB code
3ojx
Structure name
disulfide crosslinked cytochrome p450 reductase inactive
Structure deposition date
2010-08-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
75
Minimum pKa ?
8
% buried
100
Peptide accession
P00388
Residue number A
147
Residue number B
363
Peptide name
NADPH--cytochrome P450 reductase

Ligandability

Cysteine 147 of NADPH--cytochrome P450 reductase

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 363 of NADPH--cytochrome P450 reductase

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 147 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 514 has been assigned to correct residue.
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