Glutamate receptor 3
Intermolecular
Cysteine 78 of Glutamate receptor 2 and cysteine 334
Cysteine 334 and cysteine 334
Cysteine 330 of Glutamate receptor 2 and cysteine 334
Cysteine 78 of Glutamate receptor 2 and cysteine 85
Cysteine 85 and cysteine 111
Cysteine 330 of Glutamate receptor 2 and cysteine 85
Cysteine 85 and cysteine 85
Cysteine 334 and cysteine 85
Intramolecular
Cysteine 744 and cysteine 799
Cysteine 111 and cysteine 334
5fwy A 57 B 312
A redox-regulated disulphide may form between cysteine 78 of Glutamate receptor 2 and cysteine 334 of Glutamate receptor 3 (57 and 312 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
5fwy
Structure name
crystal structure of the ampa receptor glua2/a3 n-terminal domain heterodimer
Structure deposition date
2016-02-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glutamate receptor 2
Peptide B name
Glutamate receptor 3
Peptide A accession
P19491
Peptide B accession
P19492
Peptide A residue number
78
Peptide B residue number
334
Ligandability
Cysteine 78 of Glutamate receptor 2
Cysteine 334 of Glutamate receptor 3
3o21 C 312 D 312
A redox-regulated disulphide may form between two units of Glutamate receptor 3 at cysteines 334 and 334 (312 and 312 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
3o21
Structure name
high resolution structure of glua3 n-terminal domain (ntd)
Structure deposition date
2010-07-22
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glutamate receptor 3
Peptide B name
Glutamate receptor 3
Peptide A accession
P19492
Peptide B accession
P19492
Peptide A residue number
334
Peptide B residue number
334
Ligandability
5fwy C 309 D 312
A redox-regulated disulphide may form between cysteine 330 of Glutamate receptor 2 and cysteine 334 of Glutamate receptor 3 (309 and 312 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
5fwy
Structure name
crystal structure of the ampa receptor glua2/a3 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 3
Peptide A accession
P19491
Peptide B accession
P19492
Peptide A residue number
330
Peptide B residue number
334
Ligandability
Cysteine 330 of Glutamate receptor 2
Cysteine 334 of Glutamate receptor 3
5fwy A 57 B 63
A redox-regulated disulphide may form between cysteine 78 of Glutamate receptor 2 and cysteine 85 of Glutamate receptor 3 (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 ?
44
PDB code
5fwy
Structure name
crystal structure of the ampa receptor glua2/a3 n-terminal domain heterodimer
Structure deposition date
2016-02-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glutamate receptor 2
Peptide B name
Glutamate receptor 3
Peptide A accession
P19491
Peptide B accession
P19492
Peptide A residue number
78
Peptide B residue number
85
Ligandability
Cysteine 78 of Glutamate receptor 2
Cysteine 85 of Glutamate receptor 3
6fpj A 63 C 312
A redox-regulated disulphide may form between two units of Glutamate receptor 3 at cysteines 85 and 111 (63 and 312 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
6fpj
Structure name
structure of the ampar glua3 n-terminal domain bound to phosphate
Structure deposition date
2018-02-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glutamate receptor 3
Peptide B name
Glutamate receptor 3
Peptide A accession
P19492
Peptide B accession
P19492
Peptide A residue number
85
Peptide B residue number
111
Ligandability
Cysteine 85 of Glutamate receptor 3
Cysteine 111 of Glutamate receptor 3
Uncertain whether structure cysteine 312 has been assigned to correct residue.
5fwy C 309 D 63
A redox-regulated disulphide may form between cysteine 330 of Glutamate receptor 2 and cysteine 85 of Glutamate receptor 3 (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 ?
42
PDB code
5fwy
Structure name
crystal structure of the ampa receptor glua2/a3 n-terminal domain heterodimer
Structure deposition date
2016-02-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glutamate receptor 2
Peptide B name
Glutamate receptor 3
Peptide A accession
P19491
Peptide B accession
P19492
Peptide A residue number
330
Peptide B residue number
85
Ligandability
Cysteine 330 of Glutamate receptor 2
Cysteine 85 of Glutamate receptor 3
6fpj A 63 C 63
A redox-regulated disulphide may form between two units of Glutamate receptor 3 at cysteines 85 and 85 (63 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 ?
39
PDB code
6fpj
Structure name
structure of the ampar glua3 n-terminal domain bound to phosphate
Structure deposition date
2018-02-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glutamate receptor 3
Peptide B name
Glutamate receptor 3
Peptide A accession
P19492
Peptide B accession
P19492
Peptide A residue number
85
Peptide B residue number
85
Ligandability
3p3w A 312 C 63
A redox-regulated disulphide may form between two units of Glutamate receptor 3 at cysteines 334 and 85 (312 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 ?
39
PDB code
3p3w
Structure name
structure of a dimeric glua3 n-terminal domain (ntd) at 4
Structure deposition date
2010-10-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide A name
Glutamate receptor 3
Peptide B name
Glutamate receptor 3
Peptide A accession
P19492
Peptide B accession
P19492
Peptide A residue number
334
Peptide B residue number
85
Ligandability
Cysteine 334 of Glutamate receptor 3
Cysteine 85 of Glutamate receptor 3
3dp4 A 206 A 261
A redox-regulated disulphide may form within Glutamate receptor 3 between cysteines 744 and 799 (206 and 261 respectively in this structure).
Details
Redox score ?
91
PDB code
3dp4
Structure name
crystal structure of the binding domain of the ampa subunit glur3 bound to ampa
Structure deposition date
2008-07-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19492
Residue number A
744
Residue number B
799
Peptide name
Glutamate receptor 3
Ligandability
Cysteine 744 of Glutamate receptor 3
Cysteine 799 of Glutamate receptor 3
3o21 B 89 B 312
A redox-regulated disulphide may form within Glutamate receptor 3 between cysteines 111 and 334 (89 and 312 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
30
PDB code
3o21
Structure name
high resolution structure of glua3 n-terminal domain (ntd)
Structure deposition date
2010-07-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
nan
Peptide accession
P19492
Residue number A
111
Residue number B
334
Peptide name
Glutamate receptor 3
Ligandability
Cysteine 111 of Glutamate receptor 3
Cysteine 334 of Glutamate receptor 3
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