ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glutamate receptor

Intermolecular
Cysteine 549 and cysteine 9 of Protein cornichon homolog 2
Cysteine 549 and cysteine 84 of Protein cornichon homolog 2
Intramolecular
Cysteine 739 and cysteine 794
A redox-regulated disulphide may form between cysteine 549 of Glutamate receptor and cysteine 9 of Protein cornichon homolog 2 (528 and 9 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7lep
Structure name
the composite lbd-tmd structure combined from all hippocampal ampar subtypes at 3
Structure deposition date
2021-01-14
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
86
Peptide A name
Glutamate receptor
Peptide B name
Protein cornichon homolog 2
Peptide A accession
C9K0Z0
Peptide B accession
O35089
Peptide A residue number
549
Peptide B residue number
9

Ligandability

Cysteine 549 of Glutamate receptor

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 9 of Protein cornichon homolog 2

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 between cysteine 549 of Glutamate receptor and cysteine 84 of Protein cornichon homolog 2 (528 and 84 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7lep
Structure name
the composite lbd-tmd structure combined from all hippocampal ampar subtypes at 3
Structure deposition date
2021-01-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
51
Peptide A name
Glutamate receptor
Peptide B name
Protein cornichon homolog 2
Peptide A accession
C9K0Z0
Peptide B accession
O35089
Peptide A residue number
549
Peptide B residue number
84

Ligandability

Cysteine 549 of Glutamate receptor

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 84 of Protein cornichon homolog 2

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 receptor between cysteines 739 and 794 (718 and 773 respectively in this structure).

Details

Redox score ?
85
PDB code
7lep
Structure name
the composite lbd-tmd structure combined from all hippocampal ampar subtypes at 3
Structure deposition date
2021-01-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
C9K0Z0
Residue number A
739
Residue number B
794
Peptide name
Glutamate receptor

Ligandability

Cysteine 739 of Glutamate receptor

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 794 of Glutamate receptor

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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