ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Aldo-keto reductase family 1 member C2

Intermolecular
Cysteine 7 and cysteine 7
Intramolecular
Cysteine 193 and cysteine 206
Cysteine 188 and cysteine 206
A redox-regulated disulphide may form between two units of Aldo-keto reductase family 1 member C2 at cysteines 7 and 7. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
4xo6
Structure name
crystal structure of human 3-alpha hydroxysteroid dehydrogenase type 3 in complex with nadp+, 5alpha-androstan-3,17-dione and (3beta, 5alpha)-3-hydroxyandrostan-17-one
Structure deposition date
2015-01-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
100
Peptide A name
Aldo-keto reductase family 1 member C2
Peptide B name
Aldo-keto reductase family 1 member C2
Peptide A accession
P52895
Peptide B accession
P52895
Peptide A residue number
7
Peptide B residue number
7

Ligandability

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 Aldo-keto reductase family 1 member C2 between cysteines 193 and 206. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
1ihi
Structure name
crystal structure of human type iii 3-alpha-hydroxysteroid dehydrogenase/bile acid binding protein (akr1c2) complexed with nadp+ and ursodeoxycholate
Structure deposition date
2001-04-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
10
% buried
100
Peptide accession
P52895
Residue number A
193
Residue number B
206
Peptide name
Aldo-keto reductase family 1 member C2

Ligandability

Cysteine 193 of Aldo-keto reductase family 1 member C2

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 206 of Aldo-keto reductase family 1 member C2

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 Aldo-keto reductase family 1 member C2 between cysteines 188 and 206. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
4xo6
Structure name
crystal structure of human 3-alpha hydroxysteroid dehydrogenase type 3 in complex with nadp+, 5alpha-androstan-3,17-dione and (3beta, 5alpha)-3-hydroxyandrostan-17-one
Structure deposition date
2015-01-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
P52895
Residue number A
188
Residue number B
206
Peptide name
Aldo-keto reductase family 1 member C2

Ligandability

Cysteine 188 of Aldo-keto reductase family 1 member C2

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 206 of Aldo-keto reductase family 1 member C2

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.

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