ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glutamate receptor ionotropic, NMDA 2A

Intermolecular
Cysteine 798 of Glutamate receptor ionotropic, NMDA 1 and cysteine 429
Cysteine 79 of Glutamate receptor ionotropic, NMDA 1 and cysteine 320
Cysteine 79 of Glutamate receptor ionotropic, NMDA 1 and cysteine 87
Intramolecular
Cysteine 87 and cysteine 320
Cysteine 429 and cysteine 455
Cysteine 745 and cysteine 800
Cysteine 436 and cysteine 456
Cysteine 429 and cysteine 436
Cysteine 436 and cysteine 455
Cysteine 429 and cysteine 456
More...
Cysteine 455 and cysteine 456
Cysteine 456 and cysteine 460
A redox-regulated disulphide may form between cysteine 798 of Glutamate receptor ionotropic, NMDA 1 and cysteine 429 of Glutamate receptor ionotropic, NMDA 2A (698 and 794 respectively in this structure).

Details

Redox score ?
83
PDB code
7eoq
Structure name
structure of the human glun1/glun2a nmda receptor in the glycine/cpp bound state
Structure deposition date
2021-04-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glutamate receptor ionotropic, NMDA 1
Peptide B name
Glutamate receptor ionotropic, NMDA 2A
Peptide A accession
Q05586
Peptide B accession
Q12879
Peptide A residue number
798
Peptide B residue number
429

Ligandability

Cysteine 798 of Glutamate receptor ionotropic, NMDA 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 429 of Glutamate receptor ionotropic, NMDA 2A

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 79 of Glutamate receptor ionotropic, NMDA 1 and cysteine 320 of Glutamate receptor ionotropic, NMDA 2A. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6mmb
Structure name
diheteromeric nmda receptor glun1/glun2a in the 'super-splayed' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at ph 6
Structure deposition date
2018-09-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
12
% buried
nan
Peptide A name
Glutamate receptor ionotropic, NMDA 1
Peptide B name
Glutamate receptor ionotropic, NMDA 2A
Peptide A accession
P35439
Peptide B accession
Q00959
Peptide A residue number
79
Peptide B residue number
320

Ligandability

Cysteine 79 of Glutamate receptor ionotropic, NMDA 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 320 of Glutamate receptor ionotropic, NMDA 2A

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 79 of Glutamate receptor ionotropic, NMDA 1 and cysteine 87 of Glutamate receptor ionotropic, NMDA 2A. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
6mml
Structure name
diheteromeric nmda receptor glun1/glun2a in the '2-knuckle-asymmetric' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at ph 7
Structure deposition date
2018-09-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
13
% buried
nan
Peptide A name
Glutamate receptor ionotropic, NMDA 1
Peptide B name
Glutamate receptor ionotropic, NMDA 2A
Peptide A accession
P35439
Peptide B accession
Q00959
Peptide A residue number
79
Peptide B residue number
87

Ligandability

Cysteine 79 of Glutamate receptor ionotropic, NMDA 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 87 of Glutamate receptor ionotropic, NMDA 2A

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 ionotropic, NMDA 2A between cysteines 87 and 320.

Details

Redox score ?
84
PDB code
7eu7
Structure name
structure of the human glun1-glun2a nmda receptor in complex with s- ketamine, glycine and glutamate
Structure deposition date
2021-05-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q12879
Residue number A
87
Residue number B
320
Peptide name
Glutamate receptor ionotropic, NMDA 2A

Ligandability

Cysteine 87 of Glutamate receptor ionotropic, NMDA 2A

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 320 of Glutamate receptor ionotropic, NMDA 2A

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 ionotropic, NMDA 2A between cysteines 429 and 455 (32 and 58 respectively in this structure).

Details

Redox score ?
84
PDB code
6uzg
Structure name
crystal structure of glun1/glun2a-4m mutant ligand-binding domain in complex with glycine and homoquinolinic acid
Structure deposition date
2019-11-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q00959
Residue number A
429
Residue number B
455
Peptide name
Glutamate receptor ionotropic, NMDA 2A

Ligandability

Cysteine 429 of Glutamate receptor ionotropic, NMDA 2A

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 455 of Glutamate receptor ionotropic, NMDA 2A

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 ionotropic, NMDA 2A between cysteines 745 and 800.

Details

Redox score ?
81
PDB code
6mmx
Structure name
triheteromeric nmda receptor glun1/glun2a/glun2a* in the 'extended' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at ph 7
Structure deposition date
2018-10-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
28
Peptide accession
Q00959
Residue number A
745
Residue number B
800
Peptide name
Glutamate receptor ionotropic, NMDA 2A

Ligandability

Cysteine 745 of Glutamate receptor ionotropic, NMDA 2A

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 800 of Glutamate receptor ionotropic, NMDA 2A

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 ionotropic, NMDA 2A between cysteines 436 and 456.

Details

Redox score ?
79
PDB code
6mmn
Structure name
diheteromeric nmda receptor glun1/glun2a in the '2-knuckle-symmetric' conformation, in complex with glycine and glutamate, in the presence of 1 micromolar zinc chloride, and at ph 8
Structure deposition date
2018-10-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
7
% buried
59
Peptide accession
Q00959
Residue number A
436
Residue number B
456
Peptide name
Glutamate receptor ionotropic, NMDA 2A

Ligandability

Cysteine 436 of Glutamate receptor ionotropic, NMDA 2A

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 456 of Glutamate receptor ionotropic, NMDA 2A

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 ionotropic, NMDA 2A between cysteines 429 and 436 (32 and 39 respectively in this structure).

Details

Redox score ?
62
PDB code
4nf6
Structure name
crystal structure of glun1/glun2a ligand-binding domain in complex with glycine and ppda
Structure deposition date
2013-10-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q00959
Residue number A
429
Residue number B
436
Peptide name
Glutamate receptor ionotropic, NMDA 2A

Ligandability

Cysteine 429 of Glutamate receptor ionotropic, NMDA 2A

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 436 of Glutamate receptor ionotropic, NMDA 2A

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 ionotropic, NMDA 2A between cysteines 436 and 455 (38 and 57 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
5h8n
Structure name
structure of the human glun1/glun2a lbd in complex with nam
Structure deposition date
2015-12-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q12879
Residue number A
436
Residue number B
455
Peptide name
Glutamate receptor ionotropic, NMDA 2A

Ligandability

Cysteine 436 of Glutamate receptor ionotropic, NMDA 2A

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 455 of Glutamate receptor ionotropic, NMDA 2A

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 ionotropic, NMDA 2A between cysteines 429 and 456 (32 and 59 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
5i57
Structure name
glutamate- and glycine-bound glun1/glun2a agonist binding domains
Structure deposition date
2016-02-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q00959
Residue number A
429
Residue number B
456
Peptide name
Glutamate receptor ionotropic, NMDA 2A

Ligandability

Cysteine 429 of Glutamate receptor ionotropic, NMDA 2A

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 456 of Glutamate receptor ionotropic, NMDA 2A

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 ionotropic, NMDA 2A between cysteines 455 and 456 (58 and 59 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
6uzx
Structure name
crystal structure of glun1/glun2a-4m mutant ligand-binding domain in complex with glycine and ubp791
Structure deposition date
2019-11-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q00959
Residue number A
455
Residue number B
456
Peptide name
Glutamate receptor ionotropic, NMDA 2A

Ligandability

Cysteine 455 of Glutamate receptor ionotropic, NMDA 2A

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 456 of Glutamate receptor ionotropic, NMDA 2A

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 ionotropic, NMDA 2A between cysteines 456 and 460. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7eou
Structure name
structure of the human glun1/glun2a nmda receptor in the glycine/glutamate/gne-6901/9-aa bound state
Structure deposition date
2021-04-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
89
Peptide accession
Q12879
Residue number A
456
Residue number B
460
Peptide name
Glutamate receptor ionotropic, NMDA 2A

Ligandability

Cysteine 456 of Glutamate receptor ionotropic, NMDA 2A

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 460 of Glutamate receptor ionotropic, NMDA 2A

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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