Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5CBS

Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (R)-2-amino-3-(3'-hydroxybiphenyl-3-yl)propanoic acid at 1.8A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0015276	molecular_function	ligand-gated monoatomic ion channel activity
A	0016020	cellular_component	membrane
B	0015276	molecular_function	ligand-gated monoatomic ion channel activity
B	0016020	cellular_component	membrane
C	0015276	molecular_function	ligand-gated monoatomic ion channel activity
C	0016020	cellular_component	membrane
D	0015276	molecular_function	ligand-gated monoatomic ion channel activity
D	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue E42 A 301

Chain	Residue
A	TYR58
A	LYS215
A	TYR217
A	EDO304
A	HOH450
A	HOH541
A	PRO86
A	LEU87
A	THR88
A	ARG93
A	ILE108
A	SER139
A	GLU190
A	ASP213

site_id	AC2
Number of Residues	4
Details	binding site for residue SO4 A 302

Chain	Residue
A	LYS47
A	ARG145
A	TRP156
A	ARG160

site_id	AC3
Number of Residues	8
Details	binding site for residue SO4 A 303

Chain	Residue
A	MET16
A	HIS20
A	GLU21
A	ARG28
A	HOH425
A	HOH474
A	HOH624
C	HIS43

site_id	AC4
Number of Residues	7
Details	binding site for residue EDO A 304

Chain	Residue
A	TYR58
A	GLU190
A	TYR217
A	E42301
A	HOH429
A	HOH445
A	HOH475

site_id	AC5
Number of Residues	8
Details	binding site for residue EDO A 305

Chain	Residue
A	PRO102
A	PHE103
A	MET104
A	SER105
A	ASN239
A	HOH412
A	HOH629
C	SER214

site_id	AC6
Number of Residues	4
Details	binding site for residue EDO A 306

Chain	Residue
A	SER137
A	GLY138
A	HOH437
A	HOH519

site_id	AC7
Number of Residues	3
Details	binding site for residue EDO A 307

Chain	Residue
A	LYS113
A	HOH410
D	LYS79

site_id	AC8
Number of Residues	7
Details	binding site for residue GOL A 308

Chain	Residue
A	GLU24
A	GLY25
A	ARG28
A	LYS49
A	HOH604
A	HOH615
C	GLN241

site_id	AC9
Number of Residues	13
Details	binding site for residue E42 B 301

Chain	Residue
B	TYR58
B	PRO86
B	LEU87
B	THR88
B	ARG93
B	ILE108
B	SER139
B	GLU190
B	ASP213
B	LYS215
B	EDO304
B	HOH422
B	HOH557

site_id	AD1
Number of Residues	5
Details	binding site for residue SO4 B 302

Chain	Residue
B	HIS20
B	GLU21
B	ARG28
B	HIS43
B	HOH471

site_id	AD2
Number of Residues	4
Details	binding site for residue SO4 B 303

Chain	Residue
B	ARG145
B	TRP156
B	ARG160
D	LYS47

site_id	AD3
Number of Residues	6
Details	binding site for residue EDO B 304

Chain	Residue
B	TYR58
B	GLU190
B	TYR217
B	E42301
B	HOH443
B	HOH573

site_id	AD4
Number of Residues	7
Details	binding site for residue EDO B 305

Chain	Residue
B	SER214
B	HOH555
D	PRO102
D	SER105
D	ASN239
D	EDO307
D	HOH425

site_id	AD5
Number of Residues	9
Details	binding site for residue EDO B 306

Chain	Residue
B	PRO102
B	PHE103
B	MET104
B	SER105
B	HOH412
B	HOH535
B	HOH580
D	SER214
D	HOH401

site_id	AD6
Number of Residues	4
Details	binding site for residue EDO B 307

Chain	Residue
B	SER137
B	GLY138
B	HOH437
B	HOH477

site_id	AD7
Number of Residues	6
Details	binding site for residue EDO B 308

Chain	Residue
B	SER105
B	SER191
B	GLU195
B	ASN211
B	HOH519
B	HOH609

site_id	AD8
Number of Residues	8
Details	binding site for residue GOL B 309

Chain	Residue
B	GLU24
B	GLY25
B	ARG28
B	LYS49
B	HOH603
D	ARG146
D	LYS148
D	HOH629

site_id	AD9
Number of Residues	13
Details	binding site for residue E42 C 301

Chain	Residue
C	TYR58
C	PRO86
C	LEU87
C	THR88
C	ARG93
C	LEU106
C	ILE108
C	SER139
C	GLU190
C	ASP213
C	TYR217
C	HOH424
C	HOH443

site_id	AE1
Number of Residues	6
Details	binding site for residue SO4 C 302

Chain	Residue
A	HIS43
C	HIS20
C	GLU21
C	ARG28
C	GOL305
C	HOH434

site_id	AE2
Number of Residues	7
Details	binding site for residue SO4 C 303

Chain	Residue
C	SER105
C	SER191
C	GLU195
C	ASN211
C	LYS248
C	HOH478
C	HOH629

site_id	AE3
Number of Residues	3
Details	binding site for residue SO4 C 304

Chain	Residue
C	ARG145
C	TRP156
C	ARG160

site_id	AE4
Number of Residues	8
Details	binding site for residue GOL C 305

Chain	Residue
A	HIS43
A	LYS237
A	GLN241
C	LEU23
C	ARG28
C	SO4302
C	HOH434
C	HOH594

site_id	AE5
Number of Residues	9
Details	binding site for residue GOL C 306

Chain	Residue
C	LYS17
C	ASN26
C	GLU27
C	TYR29
C	GLU30
C	VAL34
C	HOH429
C	HOH439
C	HOH445

site_id	AE6
Number of Residues	3
Details	binding site for residue CL C 307

Chain	Residue
C	SER137
C	GLY138
C	HOH627

site_id	AE7
Number of Residues	14
Details	binding site for residue E42 D 301

Chain	Residue
D	TYR58
D	PRO86
D	LEU87
D	THR88
D	ARG93
D	ILE108
D	SER139
D	GLU190
D	ASP213
D	LYS215
D	TYR217
D	EDO305
D	HOH411
D	HOH547

site_id	AE8
Number of Residues	5
Details	binding site for residue SO4 D 302

Chain	Residue
D	SER105
D	SER191
D	GLU195
D	ASN211
D	HOH492

site_id	AE9
Number of Residues	7
Details	binding site for residue SO4 D 303

Chain	Residue
D	HIS20
D	GLU21
D	ARG28
D	HIS43
D	HOH466
D	HOH476
D	HOH561

site_id	AF1
Number of Residues	4
Details	binding site for residue SO4 D 304

Chain	Residue
D	ARG145
D	TRP156
D	ARG160
D	HOH552

site_id	AF2
Number of Residues	7
Details	binding site for residue EDO D 305

Chain	Residue
D	TYR58
D	GLU190
D	MET193
D	TYR217
D	E42301
D	HOH416
D	HOH555

site_id	AF3
Number of Residues	4
Details	binding site for residue EDO D 306

Chain	Residue
D	SER137
D	GLY138
D	HOH464
D	HOH572

site_id	AF4
Number of Residues	7
Details	binding site for residue EDO D 307

Chain	Residue
B	EDO305
D	MET104
D	SER105
D	ASP245
D	HOH402
D	HOH407
D	HOH425

site_id	AF5
Number of Residues	4
Details	binding site for residue EDO D 308

Chain	Residue
D	MET15
D	MET16
D	HOH405
D	HOH460

site_id	AF6
Number of Residues	4
Details	binding site for residue EDO D 309

Chain	Residue
D	ASN249
D	ASP254
D	HOH414
D	HOH627

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:11086992, ECO:0000269\|PubMed:16483599, ECO:0007744\|PDB:1FTJ, ECO:0007744\|PDB:2CMO

Chain	Residue	Details
A	PRO86
B	SER139
B	THR140
B	GLU190
C	PRO86
C	THR88
C	ARG93
C	SER139
C	THR140
C	GLU190
D	PRO86
A	THR88
D	THR88
D	ARG93
D	SER139
D	THR140
D	GLU190
A	ARG93
A	SER139
A	THR140
A	GLU190
B	PRO86
B	THR88
B	ARG93

site_id	SWS_FT_FI2
Number of Residues	12
Details	SITE: Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269\|PubMed:25103405

Chain	Residue	Details
A	ARG61
D	ARG61
D	ARG145
D	LYS237
A	ARG145
A	LYS237
B	ARG61
B	ARG145
B	LYS237
C	ARG61
C	ARG145
C	LYS237

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Crucial to convey clamshell closure to channel opening => ECO:0000269\|PubMed:25103405

Chain	Residue	Details
A	ILE118
B	ILE118
C	ILE118
D	ILE118

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKC => ECO:0000269\|PubMed:8848293

Chain	Residue	Details
A	SER147
B	SER147
C	SER147
D	SER147

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKG => ECO:0000269\|PubMed:8848293

Chain	Residue	Details
A	SER181
B	SER181
C	SER181
D	SER181

site_id	SWS_FT_FI6
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN0
B	ASN0
C	ASN0
D	ASN0

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)