Glutamate receptor
Intramolecular
Cysteine 745 and cysteine 800
Cysteine 429 and cysteine 455
Cysteine 436 and cysteine 456
Cysteine 429 and cysteine 436
Cysteine 436 and cysteine 455
Cysteine 429 and cysteine 456
Cysteine 455 and cysteine 456
6odl A 229 A 284
A redox-regulated disulphide may form within Glutamate receptor between cysteines 745 and 800 (229 and 284 respectively in this structure).
Details
Redox score ?
89
PDB code
6odl
Structure name
crystal structure of glun2a agonist binding domain with 4-butyl-(s)- ccg-iv
Structure deposition date
2019-03-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
G3V9C5
Residue number A
745
Residue number B
800
Peptide name
Glutamate receptor
Ligandability
Cysteine 745 of Glutamate receptor
Cysteine 800 of Glutamate receptor
6odl B 32 B 58
A redox-regulated disulphide may form within Glutamate receptor between cysteines 429 and 455 (32 and 58 respectively in this structure).
Details
Redox score ?
84
PDB code
6odl
Structure name
crystal structure of glun2a agonist binding domain with 4-butyl-(s)- ccg-iv
Structure deposition date
2019-03-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
G3V9C5
Residue number A
429
Residue number B
455
Peptide name
Glutamate receptor
Ligandability
Cysteine 429 of Glutamate receptor
Cysteine 455 of Glutamate receptor
6odl A 39 A 59
A redox-regulated disulphide may form within Glutamate receptor between cysteines 436 and 456 (39 and 59 respectively in this structure).
Details
Redox score ?
84
PDB code
6odl
Structure name
crystal structure of glun2a agonist binding domain with 4-butyl-(s)- ccg-iv
Structure deposition date
2019-03-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
G3V9C5
Residue number A
436
Residue number B
456
Peptide name
Glutamate receptor
Ligandability
Cysteine 436 of Glutamate receptor
Cysteine 456 of Glutamate receptor
5vii B 32 B 39
A redox-regulated disulphide may form within Glutamate receptor between cysteines 429 and 436 (32 and 39 respectively in this structure).
Details
Redox score ?
61
PDB code
5vii
Structure name
crystal structure of glun1/glun2a nmda receptor agonist binding domains with glycine and antagonist, 4-(3-fluoropropyl)phenyl-acepc
Structure deposition date
2017-04-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
G3V9C5
Residue number A
429
Residue number B
436
Peptide name
Glutamate receptor
Ligandability
Cysteine 429 of Glutamate receptor
Cysteine 436 of Glutamate receptor
6odl A 39 A 58
A redox-regulated disulphide may form within Glutamate receptor between cysteines 436 and 455 (39 and 58 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
6odl
Structure name
crystal structure of glun2a agonist binding domain with 4-butyl-(s)- ccg-iv
Structure deposition date
2019-03-26
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
G3V9C5
Residue number A
436
Residue number B
455
Peptide name
Glutamate receptor
Ligandability
Cysteine 436 of Glutamate receptor
Cysteine 455 of Glutamate receptor
5vii B 32 B 59
A redox-regulated disulphide may form within Glutamate receptor 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 ?
53
PDB code
5vii
Structure name
crystal structure of glun1/glun2a nmda receptor agonist binding domains with glycine and antagonist, 4-(3-fluoropropyl)phenyl-acepc
Structure deposition date
2017-04-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
G3V9C5
Residue number A
429
Residue number B
456
Peptide name
Glutamate receptor
Ligandability
Cysteine 429 of Glutamate receptor
Cysteine 456 of Glutamate receptor
6odl A 58 A 59
A redox-regulated disulphide may form within Glutamate receptor 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
6odl
Structure name
crystal structure of glun2a agonist binding domain with 4-butyl-(s)- ccg-iv
Structure deposition date
2019-03-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
G3V9C5
Residue number A
455
Residue number B
456
Peptide name
Glutamate receptor
Ligandability
Cysteine 455 of Glutamate receptor
Cysteine 456 of Glutamate receptor
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