Glutamate receptor 4
Intermolecular
Cysteine 78 of Glutamate receptor 2 and cysteine 331
Cysteine 78 of Glutamate receptor 2 and cysteine 84
Cysteine 330 of Glutamate receptor 2 and cysteine 331
Cysteine 330 of Glutamate receptor 2 and cysteine 84
Intramolecular
Cysteine 740 and cysteine 795
Cysteine 84 and cysteine 331
Cysteine 185 and cysteine 213
Cysteine 740 and cysteine 259
5fwx C 57 D 310
A redox-regulated disulphide may form between cysteine 78 of Glutamate receptor 2 and cysteine 331 of Glutamate receptor 4 (57 and 310 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
5fwx
Structure name
crystal structure of the ampa receptor glua2/a4 n-terminal domain heterodimer
Structure deposition date
2016-02-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glutamate receptor 2
Peptide B name
Glutamate receptor 4
Peptide A accession
P19491
Peptide B accession
P19493
Peptide A residue number
78
Peptide B residue number
331
Ligandability
Cysteine 78 of Glutamate receptor 2
Cysteine 331 of Glutamate receptor 4
5fwx C 57 D 63
A redox-regulated disulphide may form between cysteine 78 of Glutamate receptor 2 and cysteine 84 of Glutamate receptor 4 (57 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 ?
45
PDB code
5fwx
Structure name
crystal structure of the ampa receptor glua2/a4 n-terminal domain heterodimer
Structure deposition date
2016-02-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glutamate receptor 2
Peptide B name
Glutamate receptor 4
Peptide A accession
P19491
Peptide B accession
P19493
Peptide A residue number
78
Peptide B residue number
84
Ligandability
Cysteine 78 of Glutamate receptor 2
Cysteine 84 of Glutamate receptor 4
5fwx A 309 B 310
A redox-regulated disulphide may form between cysteine 330 of Glutamate receptor 2 and cysteine 331 of Glutamate receptor 4 (309 and 310 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
5fwx
Structure name
crystal structure of the ampa receptor glua2/a4 n-terminal domain heterodimer
Structure deposition date
2016-02-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glutamate receptor 2
Peptide B name
Glutamate receptor 4
Peptide A accession
P19491
Peptide B accession
P19493
Peptide A residue number
330
Peptide B residue number
331
Ligandability
Cysteine 330 of Glutamate receptor 2
Cysteine 331 of Glutamate receptor 4
5fwx A 309 B 63
A redox-regulated disulphide may form between cysteine 330 of Glutamate receptor 2 and cysteine 84 of Glutamate receptor 4 (309 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 ?
41
PDB code
5fwx
Structure name
crystal structure of the ampa receptor glua2/a4 n-terminal domain heterodimer
Structure deposition date
2016-02-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glutamate receptor 2
Peptide B name
Glutamate receptor 4
Peptide A accession
P19491
Peptide B accession
P19493
Peptide A residue number
330
Peptide B residue number
84
Ligandability
Cysteine 330 of Glutamate receptor 2
Cysteine 84 of Glutamate receptor 4
3fat C 204 C 259
A redox-regulated disulphide may form within Glutamate receptor 4 between cysteines 740 and 795 (204 and 259 respectively in this structure).
Details
Redox score ?
89
PDB code
3fat
Structure name
x-ray structure of iglur4 flip ligand-binding core (s1s2) in complex with (s)-ampa at 1
Structure deposition date
2008-11-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
37
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19493
Residue number A
740
Residue number B
795
Peptide name
Glutamate receptor 4
Ligandability
Cysteine 740 of Glutamate receptor 4
Cysteine 795 of Glutamate receptor 4
4gpa A 63 A 310
A redox-regulated disulphide may form within Glutamate receptor 4 between cysteines 84 and 331 (63 and 310 respectively in this structure).
Details
Redox score ?
83
PDB code
4gpa
Structure name
high resolution structure of the glua4 n-terminal domain (ntd)
Structure deposition date
2012-08-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19493
Residue number A
84
Residue number B
331
Peptide name
Glutamate receptor 4
Ligandability
Cysteine 84 of Glutamate receptor 4
Cysteine 331 of Glutamate receptor 4
5fwx B 164 B 192
A redox-regulated disulphide may form within Glutamate receptor 4 between cysteines 185 and 213 (164 and 192 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
5fwx
Structure name
crystal structure of the ampa receptor glua2/a4 n-terminal domain heterodimer
Structure deposition date
2016-02-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
87
Peptide accession
P19493
Residue number A
185
Residue number B
213
Peptide name
Glutamate receptor 4
Ligandability
Cysteine 185 of Glutamate receptor 4
Cysteine 213 of Glutamate receptor 4
3fat B 204 B 259
A redox-regulated disulphide may form within Glutamate receptor 4 between cysteines 740 and 259 (204 and 259 respectively in this structure).
Details
Redox score ?
nan
PDB code
3fat
Structure name
x-ray structure of iglur4 flip ligand-binding core (s1s2) in complex with (s)-ampa at 1
Structure deposition date
2008-11-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19493
Residue number A
740
Residue number B
259
Peptide name
Glutamate receptor 4
Ligandability
Cysteine 740 of Glutamate receptor 4
Cysteine 259 of Glutamate receptor 4
Cysteine 259 in protein B could not be asigned to a Uniprot residue.
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