5H8S

Structure of the human GluA2 LBD in complex with GNE3419

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue GLU A 301

Chain	Residue
A	TYR61
A	HOH428
A	HOH444
A	HOH466
A	PRO89
A	LEU90
A	THR91
A	ARG96
A	GLY141
A	SER142
A	THR143
A	GLU193

---

site_id	AC2
Number of Residues	19
Details	binding site for residue 5YC A 302

Chain	Residue
A	PRO105
A	MET107
A	SER108
A	SER217
A	LYS218
A	GLY219
A	SER242
A	HOH494
A	HOH528
B	ILE92
B	PRO105
B	MET107
B	SER108
B	SER217
B	LYS218
B	GLY219
B	HOH454
B	HOH477
B	HOH490

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN A 303

Chain	Residue
A	GLU42
A	HIS46
A	CAC305
C	GLU166

---

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN A 304

Chain	Residue
A	HIS23
A	HOH579
B	ASP65
B	HOH526

---

site_id	AC5
Number of Residues	9
Details	binding site for residue CAC A 305

Chain	Residue
A	GLU42
A	HIS46
A	ZN303
A	HOH401
C	ARG163
C	ALA165
C	GLU166
C	SER168
C	PHE170

---

site_id	AC6
Number of Residues	13
Details	binding site for residue GLU C 301

Chain	Residue
C	TYR61
C	PRO89
C	LEU90
C	THR91
C	ARG96
C	GLY141
C	SER142
C	THR143
C	GLU193
C	TYR220
C	HOH469
C	HOH504
C	HOH509

---

site_id	AC7
Number of Residues	20
Details	binding site for residue 5YC C 302

Chain	Residue
C	ILE92
C	ILE92
C	PRO105
C	PRO105
C	MET107
C	MET107
C	SER108
C	SER108
C	SER217
C	SER217
C	LYS218
C	LYS218
C	GLY219
C	GLY219
C	HOH419
C	HOH419
C	HOH496
C	HOH496
C	HOH549
C	HOH549

---

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN C 303

Chain	Residue
B	HIS23
C	HIS23
C	GLU30
C	HOH618

---

site_id	AC9
Number of Residues	5
Details	binding site for residue ZN C 304

Chain	Residue
A	GLU166
C	GLU42
C	HIS46
C	LEU241
C	HOH607

---

site_id	AD1
Number of Residues	14
Details	binding site for residue GLU B 301

Chain	Residue
B	GLU193
B	TYR220
B	HOH431
B	HOH447
B	HOH452
B	TYR61
B	PRO89
B	LEU90
B	THR91
B	ARG96
B	LEU138
B	GLY141
B	SER142
B	THR143

---

site_id	AD2
Number of Residues	4
Details	binding site for residue ZN B 302

Chain	Residue
B	GLU42
B	LYS45
B	HIS46
B	HOH488

---

site_id	AD3
Number of Residues	1
Details	binding site for residue ZN B 303

Chain	Residue
B	ASP156

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:20614889, ECO:0007744|PDB:2XHD

Chain	Residue	Details
A	PRO89
B	THR91
B	SER142
B	THR143
A	THR91
A	SER142
A	THR143
C	PRO89
C	THR91
C	SER142
C	THR143
B	PRO89

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:20614889, ECO:0000269|PubMed:21531559, ECO:0007744|PDB:2XHD, ECO:0007744|PDB:3R7X

Chain	Residue	Details
A	ARG96
C	ARG96
B	ARG96

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:20614889, ECO:0000269|PubMed:21531559, ECO:0007744|PDB:2XHD

Chain	Residue	Details
A	GLU193
C	GLU193
B	GLU193

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphoserine; by PKC => ECO:0000250|UniProtKB:P19491

Chain	Residue	Details
A	SER150
C	SER150
B	SER150

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphoserine; by PKG => ECO:0000250|UniProtKB:P19491

Chain	Residue	Details
A	SER184
C	SER184
B	SER184

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN3
C	ASN3
B	ASN3

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