ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Glutamate receptor ionotropic, NMDA 2C

Intramolecular
Cysteine 82 and cysteine 317
Cysteine 433 and cysteine 454
Cysteine 426 and cysteine 453
Cysteine 433 and cysteine 453
Cysteine 453 and cysteine 454
Cysteine 426 and cysteine 433
Cysteine 743 and cysteine 798
Cysteine 426 and cysteine 454
Cysteine 454 and cysteine 458
A redox-regulated disulphide may form within Glutamate receptor ionotropic, NMDA 2C between cysteines 82 and 317.

Details

Redox score ?
86
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)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14957
Residue number A
82
Residue number B
317
Peptide name
Glutamate receptor ionotropic, NMDA 2C

Ligandability

Cysteine 82 of Glutamate receptor ionotropic, NMDA 2C

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 317 of Glutamate receptor ionotropic, NMDA 2C

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 2C between cysteines 433 and 454.

Details

Redox score ?
84
PDB code
8e98
Structure name
d-cycloserine and glutamate bound human glun1a-glun2c nmda receptor in nanodisc - intact conformation
Structure deposition date
2022-08-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14957
Residue number A
433
Residue number B
454
Peptide name
Glutamate receptor ionotropic, NMDA 2C

Ligandability

Cysteine 433 of Glutamate receptor ionotropic, NMDA 2C

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 2C

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 2C between cysteines 426 and 453.

Details

Redox score ?
83
PDB code
8e94
Structure name
pyd-106-bound human glun1a-glun2c nmda receptor in intact conformation
Structure deposition date
2022-08-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14957
Residue number A
426
Residue number B
453
Peptide name
Glutamate receptor ionotropic, NMDA 2C

Ligandability

Cysteine 426 of Glutamate receptor ionotropic, NMDA 2C

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 453 of Glutamate receptor ionotropic, NMDA 2C

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 2C between cysteines 433 and 453. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
8e94
Structure name
pyd-106-bound human glun1a-glun2c nmda receptor in intact conformation
Structure deposition date
2022-08-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14957
Residue number A
433
Residue number B
453
Peptide name
Glutamate receptor ionotropic, NMDA 2C

Ligandability

Cysteine 433 of Glutamate receptor ionotropic, NMDA 2C

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 453 of Glutamate receptor ionotropic, NMDA 2C

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 2C between cysteines 453 and 454. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
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 ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14957
Residue number A
453
Residue number B
454
Peptide name
Glutamate receptor ionotropic, NMDA 2C

Ligandability

Cysteine 453 of Glutamate receptor ionotropic, NMDA 2C

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 2C

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 2C between cysteines 426 and 433. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
8e93
Structure name
d-cycloserine and glutamate bound human glun1a-glun2c nmda receptor in splayed conformation
Structure deposition date
2022-08-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14957
Residue number A
426
Residue number B
433
Peptide name
Glutamate receptor ionotropic, NMDA 2C

Ligandability

Cysteine 426 of Glutamate receptor ionotropic, NMDA 2C

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 433 of Glutamate receptor ionotropic, NMDA 2C

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 2C between cysteines 743 and 798. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
8e93
Structure name
d-cycloserine and glutamate bound human glun1a-glun2c nmda receptor in splayed conformation
Structure deposition date
2022-08-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
0
Peptide accession
Q14957
Residue number A
743
Residue number B
798
Peptide name
Glutamate receptor ionotropic, NMDA 2C

Ligandability

Cysteine 743 of Glutamate receptor ionotropic, NMDA 2C

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 2C

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 2C between cysteines 426 and 454. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
8e94
Structure name
pyd-106-bound human glun1a-glun2c nmda receptor in intact conformation
Structure deposition date
2022-08-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14957
Residue number A
426
Residue number B
454
Peptide name
Glutamate receptor ionotropic, NMDA 2C

Ligandability

Cysteine 426 of Glutamate receptor ionotropic, NMDA 2C

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 2C

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 2C between cysteines 454 and 458. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
8e97
Structure name
pyd-106-bound human glun1a-glun2c nmda receptor in splayed conformation
Structure deposition date
2022-08-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
nan
Peptide accession
Q14957
Residue number A
454
Residue number B
458
Peptide name
Glutamate receptor ionotropic, NMDA 2C

Ligandability

Cysteine 454 of Glutamate receptor ionotropic, NMDA 2C

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 458 of Glutamate receptor ionotropic, NMDA 2C

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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