ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glutamate receptor ionotropic, NMDA 1

Intermolecular
Cysteine 798 and cysteine 429 of Glutamate receptor ionotropic, NMDA 2A
Cysteine 79 and cysteine 320 of Glutamate receptor ionotropic, NMDA 2A
Cysteine 79 and cysteine 87 of Glutamate receptor ionotropic, NMDA 2A
Intramolecular
Cysteine 744 and cysteine 291
Cysteine 744 and cysteine 798
Cysteine 420 and cysteine 454
Cysteine 436 and cysteine 455
Cysteine 79 and cysteine 308
Cysteine 420 and cysteine 436
Cysteine 436 and cysteine 454
More...
Cysteine 420 and cysteine 455
Cysteine 454 and cysteine 455
Cysteine 436 and cysteine 459
Cysteine 455 and cysteine 459
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 1 between cysteines 744 and 291 (237 and 291 respectively in this structure).

Details

Redox score ?
88
PDB code
5tpa
Structure name
structure of the human glun1/glun2a lbd in complex with compound 9 (gne3500)
Structure deposition date
2016-10-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q05586
Residue number A
744
Residue number B
291
Peptide name
Glutamate receptor ionotropic, NMDA 1

Ligandability

Cysteine 744 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 291 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 291 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Glutamate receptor ionotropic, NMDA 1 between cysteines 744 and 798 (765 and 819 respectively in this structure).

Details

Redox score ?
84
PDB code
7teb
Structure name
cryo-em structure of glun1b-2b nmdar complexed to fab2 non-active1- like
Structure deposition date
2022-01-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
0
Peptide accession
P35439
Residue number A
744
Residue number B
798
Peptide name
Glutamate receptor ionotropic, NMDA 1

Ligandability

Cysteine 744 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 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.

A redox-regulated disulphide may form within Glutamate receptor ionotropic, NMDA 1 between cysteines 420 and 454.

Details

Redox score ?
80
PDB code
8e96
Structure name
glycine and glutamate bound human glun1a-glun2d nmda receptor
Structure deposition date
2022-08-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
12
Peptide accession
Q05586
Residue number A
420
Residue number B
454
Peptide name
Glutamate receptor ionotropic, NMDA 1

Ligandability

Cysteine 420 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 454 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.

A redox-regulated disulphide may form within Glutamate receptor ionotropic, NMDA 1 between cysteines 436 and 455 (457 and 476 respectively in this structure).

Details

Redox score ?
79
PDB code
6whv
Structure name
glun1b-glun2b nmda receptor in complex with sdz 220-040 and l689,560, class 2
Structure deposition date
2020-04-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
64
Peptide accession
P35439
Residue number A
436
Residue number B
455
Peptide name
Glutamate receptor ionotropic, NMDA 1

Ligandability

Cysteine 436 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 455 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.

A redox-regulated disulphide may form within Glutamate receptor ionotropic, NMDA 1 between cysteines 79 and 308. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
8e99
Structure name
human glun1a-glun2a-glun2c triheteromeric nmda receptor in complex with nb-4
Structure deposition date
2022-08-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
28
Peptide accession
Q05586
Residue number A
79
Residue number B
308
Peptide name
Glutamate receptor ionotropic, NMDA 1

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 308 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.

A redox-regulated disulphide may form within Glutamate receptor ionotropic, NMDA 1 between cysteines 420 and 436 (29 and 45 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
5kcj
Structure name
structure of the human glun1/glun2a lbd in complex with gne6901
Structure deposition date
2016-06-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q05586
Residue number A
420
Residue number B
436
Peptide name
Glutamate receptor ionotropic, NMDA 1

Ligandability

Cysteine 420 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 436 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.

A redox-regulated disulphide may form within Glutamate receptor ionotropic, NMDA 1 between cysteines 436 and 454 (45 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
5h8f
Structure name
structure of the apo human glun1/glun2a lbd
Structure deposition date
2015-12-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q05586
Residue number A
436
Residue number B
454
Peptide name
Glutamate receptor ionotropic, NMDA 1

Ligandability

Cysteine 436 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 454 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.

A redox-regulated disulphide may form within Glutamate receptor ionotropic, NMDA 1 between cysteines 420 and 455 (29 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
5kcj
Structure name
structure of the human glun1/glun2a lbd in complex with gne6901
Structure deposition date
2016-06-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q05586
Residue number A
420
Residue number B
455
Peptide name
Glutamate receptor ionotropic, NMDA 1

Ligandability

Cysteine 420 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 455 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.

A redox-regulated disulphide may form within Glutamate receptor ionotropic, NMDA 1 between cysteines 454 and 455 (63 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
5tp9
Structure name
structure of the human glun1/glun2a lbd in complex with compound 2 (gne9178)
Structure deposition date
2016-10-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q05586
Residue number A
454
Residue number B
455
Peptide name
Glutamate receptor ionotropic, NMDA 1

Ligandability

Cysteine 454 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 455 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.

A redox-regulated disulphide may form within Glutamate receptor ionotropic, NMDA 1 between cysteines 436 and 459. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
7eor
Structure name
structure of the human glun1/glun2a nmda receptor in the glycine/glutamate/gne-6901 bound state
Structure deposition date
2021-04-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
nan
Peptide accession
Q05586
Residue number A
436
Residue number B
459
Peptide name
Glutamate receptor ionotropic, NMDA 1

Ligandability

Cysteine 436 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 459 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.

A redox-regulated disulphide may form within Glutamate receptor ionotropic, NMDA 1 between cysteines 455 and 459. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
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)
10
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
nan
Peptide accession
Q05586
Residue number A
455
Residue number B
459
Peptide name
Glutamate receptor ionotropic, NMDA 1

Ligandability

Cysteine 455 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 459 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.

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