ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Alpha-enolase

Intramolecular
Cysteine 337 and cysteine 339 L
Cysteine 357 and cysteine 389 L
Cysteine 339 and cysteine 357 L
A redox-regulated disulphide may form within Alpha-enolase between cysteines 337 and 339 (336 and 338 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
2psn
Structure name
crystal structure of enolase1
Structure deposition date
2007-05-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
93
Minimum pKa ?
13
% buried
100
Peptide accession
P06733
Residue number A
337
Residue number B
339
Peptide name
Alpha-enolase

Ligandability

Cysteine 337 of Alpha-enolase

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 339 of Alpha-enolase

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 Alpha-enolase between cysteines 357 and 389 (356 and 388 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
3b97
Structure name
crystal structure of human enolase 1
Structure deposition date
2007-11-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
84
Peptide accession
P06733
Residue number A
357
Residue number B
389
Peptide name
Alpha-enolase

Ligandability

Cysteine 357 of Alpha-enolase

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.

Cysteine 389 of Alpha-enolase

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 Alpha-enolase between cysteines 339 and 357 (338 and 356 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
3b97
Structure name
crystal structure of human enolase 1
Structure deposition date
2007-11-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
P06733
Residue number A
339
Residue number B
357
Peptide name
Alpha-enolase

Ligandability

Cysteine 339 of Alpha-enolase

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.

Cysteine 357 of Alpha-enolase

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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