ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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glutamate dehydrogenase [NAD(P)(+)]

Intramolecular
Cysteine 330 and cysteine 379
Cysteine 115 and cysteine 149
Cysteine 149 and cysteine 175
A redox-regulated disulphide may form within glutamate dehydrogenase [NAD(P)(+)] between cysteines 330 and 379. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
8ar8
Structure name
bovine glutamate dehydrogenase in complex with adp at 2
Structure deposition date
2022-08-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
96
Peptide accession
A0A140T871
Residue number A
330
Residue number B
379
Peptide name
glutamate dehydrogenase [NAD(P)(+)]

Ligandability

Cysteine 330 of glutamate dehydrogenase [NAD(P)(+)]

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 379 of glutamate dehydrogenase [NAD(P)(+)]

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 [NAD(P)(+)] between cysteines 115 and 149 (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 ?
26
PDB code
6dhq
Structure name
bovine glutamate dehydrogenase complexed with nadph, glutamate, and gtp
Structure deposition date
2018-05-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
92
Minimum pKa ?
12
% buried
100
Peptide accession
A0A140T871
Residue number A
115
Residue number B
149
Peptide name
glutamate dehydrogenase [NAD(P)(+)]

Ligandability

Cysteine 115 of glutamate dehydrogenase [NAD(P)(+)]

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 149 of glutamate dehydrogenase [NAD(P)(+)]

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 [NAD(P)(+)] between cysteines 149 and 175 (89 and 115 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
6dhk
Structure name
bovine glutamate dehydrogenase complexed with adp
Structure deposition date
2018-05-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
100
Peptide accession
A0A140T871
Residue number A
149
Residue number B
175
Peptide name
glutamate dehydrogenase [NAD(P)(+)]

Ligandability

Cysteine 149 of glutamate dehydrogenase [NAD(P)(+)]

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 175 of glutamate dehydrogenase [NAD(P)(+)]

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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