ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Mitochondrial enolase superfamily member 1

Intramolecular
Cysteine 194 and cysteine 208
Cysteine 362 and cysteine 385
Cysteine 353 and cysteine 385
A redox-regulated disulphide may form within Mitochondrial enolase superfamily member 1 between cysteines 194 and 208 (198 and 212 respectively in this structure).

Details

Redox score ?
63
PDB code
4a35
Structure name
crystal structure of human mitochondrial enolase superfamily member 1 (enosf1)
Structure deposition date
2011-09-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
77
Peptide accession
Q7L5Y1
Residue number A
194
Residue number B
208
Peptide name
Mitochondrial enolase superfamily member 1

Ligandability

Cysteine 194 of Mitochondrial enolase superfamily member 1

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 208 of Mitochondrial enolase superfamily member 1

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 Mitochondrial enolase superfamily member 1 between cysteines 362 and 385 (366 and 389 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4a35
Structure name
crystal structure of human mitochondrial enolase superfamily member 1 (enosf1)
Structure deposition date
2011-09-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
100
Peptide accession
Q7L5Y1
Residue number A
362
Residue number B
385
Peptide name
Mitochondrial enolase superfamily member 1

Ligandability

Cysteine 362 of Mitochondrial enolase superfamily member 1

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 385 of Mitochondrial enolase superfamily member 1

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 Mitochondrial enolase superfamily member 1 between cysteines 353 and 385 (357 and 389 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4a35
Structure name
crystal structure of human mitochondrial enolase superfamily member 1 (enosf1)
Structure deposition date
2011-09-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
100
Peptide accession
Q7L5Y1
Residue number A
353
Residue number B
385
Peptide name
Mitochondrial enolase superfamily member 1

Ligandability

Cysteine 353 of Mitochondrial enolase superfamily member 1

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 385 of Mitochondrial enolase superfamily member 1

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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