Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5VDI

Crystal Structure of Human Glycine Receptor alpha-3 Mutant N38Q Bound to AM-3607, Glycine, and Ivermectin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004888	molecular_function	transmembrane signaling receptor activity
A	0005216	molecular_function	monoatomic ion channel activity
A	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
A	0005886	cellular_component	plasma membrane
A	0006811	biological_process	monoatomic ion transport
A	0016020	cellular_component	membrane
A	0016594	molecular_function	glycine binding
A	0022824	molecular_function	transmitter-gated monoatomic ion channel activity
A	0034220	biological_process	monoatomic ion transmembrane transport
B	0004888	molecular_function	transmembrane signaling receptor activity
B	0005216	molecular_function	monoatomic ion channel activity
B	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
B	0005886	cellular_component	plasma membrane
B	0006811	biological_process	monoatomic ion transport
B	0016020	cellular_component	membrane
B	0016594	molecular_function	glycine binding
B	0022824	molecular_function	transmitter-gated monoatomic ion channel activity
B	0034220	biological_process	monoatomic ion transmembrane transport
C	0004888	molecular_function	transmembrane signaling receptor activity
C	0005216	molecular_function	monoatomic ion channel activity
C	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
C	0005886	cellular_component	plasma membrane
C	0006811	biological_process	monoatomic ion transport
C	0016020	cellular_component	membrane
C	0016594	molecular_function	glycine binding
C	0022824	molecular_function	transmitter-gated monoatomic ion channel activity
C	0034220	biological_process	monoatomic ion transmembrane transport
D	0004888	molecular_function	transmembrane signaling receptor activity
D	0005216	molecular_function	monoatomic ion channel activity
D	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
D	0005886	cellular_component	plasma membrane
D	0006811	biological_process	monoatomic ion transport
D	0016020	cellular_component	membrane
D	0016594	molecular_function	glycine binding
D	0022824	molecular_function	transmitter-gated monoatomic ion channel activity
D	0034220	biological_process	monoatomic ion transmembrane transport
E	0004888	molecular_function	transmembrane signaling receptor activity
E	0005216	molecular_function	monoatomic ion channel activity
E	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
E	0005886	cellular_component	plasma membrane
E	0006811	biological_process	monoatomic ion transport
E	0016020	cellular_component	membrane
E	0016594	molecular_function	glycine binding
E	0022824	molecular_function	transmitter-gated monoatomic ion channel activity
E	0034220	biological_process	monoatomic ion transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue 7C6 A 401

Chain	Residue
A	ARG27
B	LEU85
B	ASP86
A	ILE28
A	ARG29
A	PHE32
A	GLY160
A	TYR161
B	PHE13
B	ASP80
B	ASP84

site_id	AC2
Number of Residues	6
Details	binding site for residue GLY A 402

Chain	Residue
A	PHE159
A	THR204
A	HOH501
B	PHE63
B	ARG65
B	SER129

site_id	AC3
Number of Residues	7
Details	binding site for residue IVM A 403

Chain	Residue
A	SER267
A	VAL280
A	ALA288
A	LEU291
B	ILE225
B	ILE229
B	PRO230

site_id	AC4
Number of Residues	3
Details	binding site for residue ZN A 404

Chain	Residue
A	GLU192
A	ASP194
A	HIS215

site_id	AC5
Number of Residues	10
Details	binding site for residue 7C6 B 401

Chain	Residue
B	ARG27
B	ILE28
B	ARG29
B	PHE32
B	GLY160
B	TYR161
C	PHE13
C	LEU14
C	ASP84
C	LEU85

site_id	AC6
Number of Residues	8
Details	binding site for residue GLY B 402

Chain	Residue
B	PHE159
B	TYR202
B	THR204
C	PHE63
C	ARG65
C	LEU117
C	SER129
C	HOH603

site_id	AC7
Number of Residues	13
Details	binding site for residue IVM B 403

Chain	Residue
B	THR264
B	SER267
B	SER278
B	VAL280
B	ASP284
B	ALA288
B	LEU291
B	PHE295
C	ILE225
C	GLN226
C	ILE229
C	PRO230
C	LEU233

site_id	AC8
Number of Residues	3
Details	binding site for residue ZN B 404

Chain	Residue
B	GLU192
B	ASP194
B	HIS215

site_id	AC9
Number of Residues	12
Details	binding site for residue 7C6 C 401

Chain	Residue
C	ARG27
C	ILE28
C	ARG29
C	PHE32
C	GLY160
C	TYR161
D	PHE13
D	LEU14
D	TYR78
D	LEU83
D	ASP84
D	LEU85

site_id	AD1
Number of Residues	7
Details	binding site for residue GLY C 402

Chain	Residue
D	PHE159
D	TYR202
D	THR204
E	PHE63
E	ARG65
E	LEU117
E	SER129

site_id	AD2
Number of Residues	11
Details	binding site for residue IVM C 403

Chain	Residue
C	SER267
C	VAL280
C	ASP284
C	ALA288
C	LEU291
C	PHE295
D	ILE225
D	GLN226
D	ILE229
D	PRO230
D	HOH515

site_id	AD3
Number of Residues	3
Details	binding site for residue ZN C 404

Chain	Residue
C	GLU192
C	ASP194
C	HIS215

site_id	AD4
Number of Residues	10
Details	binding site for residue 7C6 D 401

Chain	Residue
D	TYR161
E	PRO10
E	PHE13
E	ASP84
E	LEU85
D	ARG27
D	ILE28
D	ARG29
D	PHE32
D	GLY160

site_id	AD5
Number of Residues	8
Details	binding site for residue GLY D 402

Chain	Residue
C	PHE159
C	TYR202
C	THR204
D	PHE63
D	ARG65
D	LEU117
D	SER129
D	HOH501

site_id	AD6
Number of Residues	11
Details	binding site for residue IVM D 403

Chain	Residue
D	THR264
D	SER267
D	VAL280
D	ALA288
D	LEU291
D	PHE295
E	ILE225
E	GLN226
E	ILE229
E	PRO230
E	LEU233

site_id	AD7
Number of Residues	3
Details	binding site for residue ZN D 404

Chain	Residue
D	GLU192
D	ASP194
D	HIS215

site_id	AD8
Number of Residues	10
Details	binding site for residue 7C6 E 401

Chain	Residue
A	PHE13
A	TYR78
A	ASP84
A	LEU85
E	ARG27
E	ARG29
E	PHE32
E	GLY160
E	TYR161
E	ASP165

site_id	AD9
Number of Residues	5
Details	binding site for residue GLY E 402

Chain	Residue
A	PHE63
A	ARG65
A	SER129
E	PHE159
E	THR204

site_id	AE1
Number of Residues	11
Details	binding site for residue IVM E 403

Chain	Residue
A	ILE225
A	ILE229
A	PRO230
A	LEU233
E	THR264
E	SER267
E	SER268
E	VAL280
E	ALA288
E	LEU291
E	PHE295

site_id	AE2
Number of Residues	3
Details	binding site for residue ZN E 404

Chain	Residue
E	GLU192
E	ASP194
E	HIS215

Functional Information from PROSITE/UniProt

site_id	PS00236
Number of Residues	15
Details	NEUROTR_ION_CHANNEL Neurotransmitter-gated ion-channels signature. CpMdLknFPmDvqtC

Chain	Residue	Details
A	CYS138-CYS152

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	105
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"26416729","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	20
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"26416729","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	100
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"26416729","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	50
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"26416729","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	100
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"26416729","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	100
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"26416729","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P23415","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	25
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26416729","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	5
Details	Site: {"description":"Important for obstruction of the ion pore in the closed conformation","evidences":[{"source":"PubMed","id":"26416729","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	5
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26416729","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5CFB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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