ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glutamate dehydrogenase 1, mitochondrial

Intramolecular
Cysteine 327 and cysteine 376
Cysteine 112 and cysteine 146
Cysteine 146 and cysteine 172 L
A redox-regulated disulphide may form within Glutamate dehydrogenase 1, mitochondrial between cysteines 327 and 376 (274 and 323 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
6dqg
Structure name
human glutamate dehydrogenase, h454y mutant
Structure deposition date
2018-06-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
94
Peptide accession
P00367
Residue number A
327
Residue number B
376
Peptide name
Glutamate dehydrogenase 1, mitochondrial

Ligandability

Cysteine 327 of Glutamate dehydrogenase 1, mitochondrial

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 376 of Glutamate dehydrogenase 1, mitochondrial

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 Glutamate dehydrogenase 1, mitochondrial between cysteines 112 and 146 (55 and 89 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
3ete
Structure name
crystal structure of bovine glutamate dehydrogenase complexed with hexachlorophene
Structure deposition date
2008-10-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
100
Peptide accession
Q3SYY0
Residue number A
112
Residue number B
146
Peptide name
Glutamate dehydrogenase 1, mitochondrial

Ligandability

Cysteine 112 of Glutamate dehydrogenase 1, mitochondrial

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 146 of Glutamate dehydrogenase 1, mitochondrial

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 Glutamate dehydrogenase 1, mitochondrial between cysteines 146 and 172 (93 and 119 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
1nr1
Structure name
crystal structure of the r463a mutant of human glutamate dehydrogenase
Structure deposition date
2003-01-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
92
Minimum pKa ?
12
% buried
100
Peptide accession
P00367
Residue number A
146
Residue number B
172
Peptide name
Glutamate dehydrogenase 1, mitochondrial

Ligandability

Cysteine 146 of Glutamate dehydrogenase 1, mitochondrial

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 172 of Glutamate dehydrogenase 1, mitochondrial

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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