ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Aldo-keto reductase family 1 member B1

Intramolecular
Cysteine 81 and cysteine 304 L
Cysteine 81 and cysteine 113
Cysteine 299 and cysteine 304 L
A redox-regulated disulphide may form within Aldo-keto reductase family 1 member B1 between cysteines 81 and 304 (80 and 303 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2fzb
Structure name
human aldose reductase complexed with four tolrestat molecules at 1
Structure deposition date
2006-02-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
94
Peptide accession
Q5U031
Residue number A
81
Residue number B
304
Peptide name
Aldo-keto reductase family 1 member B1

Ligandability

Cysteine 81 of Aldo-keto reductase family 1 member B1

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 304 of Aldo-keto reductase family 1 member B1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Aldo-keto reductase family 1 member B1 between cysteines 81 and 113 (80 and 113 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
3lep
Structure name
human aldose reductase mutant t113c in complex with idd388
Structure deposition date
2010-01-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
85
Minimum pKa ?
16
% buried
96
Peptide accession
P15121
Residue number A
81
Residue number B
113
Peptide name
Aldo-keto reductase family 1 member B1

Ligandability

Cysteine 81 of Aldo-keto reductase family 1 member B1

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 113 of Aldo-keto reductase family 1 member B1

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 113 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Aldo-keto reductase family 1 member B1 between cysteines 299 and 304 (298 and 303 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3t42
Structure name
human aldose reductase in complex with a nitrile-containing idd inhibitor
Structure deposition date
2011-07-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
11
% buried
88
Peptide accession
P15121
Residue number A
299
Residue number B
304
Peptide name
Aldo-keto reductase family 1 member B1

Ligandability

Cysteine 299 of Aldo-keto reductase family 1 member B1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 304 of Aldo-keto reductase family 1 member B1

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.

Ligandable in the dataset of Kuljanin et al.

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