ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glutamate decarboxylase-like 1

Intermolecular
Cysteine 34 and cysteine 34
Intramolecular
Cysteine 167 and cysteine 337
Cysteine 199 and cysteine 251
Cysteine 251 and cysteine 272
A redox-regulated disulphide may form between two units of Glutamate decarboxylase-like 1 at cysteines 34 and 34.

Details

Redox score ?
71
PDB code
6enz
Structure name
crystal structure of mouse gadl1
Structure deposition date
2017-10-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
8
% buried
98
Peptide A name
Glutamate decarboxylase-like 1
Peptide B name
Glutamate decarboxylase-like 1
Peptide A accession
E9QP13
Peptide B accession
E9QP13
Peptide A residue number
34
Peptide B residue number
34

Ligandability

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 decarboxylase-like 1 between cysteines 167 and 337. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6enz
Structure name
crystal structure of mouse gadl1
Structure deposition date
2017-10-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
E9QP13
Residue number A
167
Residue number B
337
Peptide name
Glutamate decarboxylase-like 1

Ligandability

Cysteine 167 of Glutamate decarboxylase-like 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 337 of Glutamate decarboxylase-like 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 Glutamate decarboxylase-like 1 between cysteines 199 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6enz
Structure name
crystal structure of mouse gadl1
Structure deposition date
2017-10-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
11
% buried
100
Peptide accession
E9QP13
Residue number A
199
Residue number B
251
Peptide name
Glutamate decarboxylase-like 1

Ligandability

Cysteine 199 of Glutamate decarboxylase-like 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 251 of Glutamate decarboxylase-like 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 Glutamate decarboxylase-like 1 between cysteines 251 and 272. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
6enz
Structure name
crystal structure of mouse gadl1
Structure deposition date
2017-10-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
98
Peptide accession
E9QP13
Residue number A
251
Residue number B
272
Peptide name
Glutamate decarboxylase-like 1

Ligandability

Cysteine 251 of Glutamate decarboxylase-like 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 272 of Glutamate decarboxylase-like 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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