Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5TIN

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

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	14
Details	binding site for residue 7C6 A 401

Chain	Residue
A	ARG27
B	LEU14
B	TYR78
B	ASP84
B	LEU85
B	ASP86
A	ILE28
A	ARG29
A	PHE32
A	GLY160
A	TYR161
A	HOH540
B	PRO10
B	PHE13

site_id	AC2
Number of Residues	8
Details	binding site for residue GLY A 402

Chain	Residue
A	PHE159
A	TYR202
A	THR204
A	PHE207
A	HOH503
B	PHE63
B	ARG65
B	SER129

site_id	AC3
Number of Residues	3
Details	binding site for residue ZN A 403

Chain	Residue
A	GLU192
A	ASP194
A	HIS215

site_id	AC4
Number of Residues	13
Details	binding site for residue 7C6 B 401

Chain	Residue
B	ARG27
B	ILE28
B	ARG29
B	PHE32
B	GLY160
B	TYR161
B	HOH541
C	PRO10
C	PHE13
C	LEU14
C	ASP84
C	LEU85
C	ASP86

site_id	AC5
Number of Residues	7
Details	binding site for residue GLY B 402

Chain	Residue
B	PHE159
B	THR204
B	PHE207
B	HOH517
C	PHE63
C	ARG65
C	SER129

site_id	AC6
Number of Residues	3
Details	binding site for residue ZN B 403

Chain	Residue
B	GLU192
B	ASP194
B	HIS215

site_id	AC7
Number of Residues	9
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	ASP84
D	LEU85

site_id	AC8
Number of Residues	3
Details	binding site for residue ZN C 403

Chain	Residue
C	GLU192
C	ASP194
C	HIS215

site_id	AC9
Number of Residues	7
Details	binding site for residue GLY C 402

Chain	Residue
C	PHE159
C	TYR202
C	THR204
C	HOH507
D	PHE63
D	ARG65
D	SER129

site_id	AD1
Number of Residues	11
Details	binding site for residue 7C6 D 401

Chain	Residue
D	ARG27
D	ILE28
D	ARG29
D	PHE32
D	GLY160
D	TYR161
E	PRO10
E	PHE13
E	ASP84
E	LEU85
E	ASP86

site_id	AD2
Number of Residues	8
Details	binding site for residue GLY D 402

Chain	Residue
D	PHE159
D	TYR202
D	THR204
D	PHE207
D	HOH603
E	PHE63
E	ARG65
E	SER129

site_id	AD3
Number of Residues	3
Details	binding site for residue ZN D 403

Chain	Residue
D	GLU192
D	ASP194
D	HIS215

site_id	AD4
Number of Residues	12
Details	binding site for residue 7C6 E 401

Chain	Residue
E	GLY160
E	TYR161
A	PRO10
A	PHE13
A	TYR78
A	ASP84
A	LEU85
A	ASP86
E	ARG27
E	ILE28
E	ARG29
E	PHE32

site_id	AD5
Number of Residues	7
Details	binding site for residue GLY E 402

Chain	Residue
A	PHE63
A	ARG65
A	SER129
E	PHE159
E	THR204
E	PHE207
E	HOH508

site_id	AD6
Number of Residues	4
Details	binding site for residue ZN E 404

Chain	Residue
E	GLU192
E	ASP194
E	HIS215
E	HOH532

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	1155
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:26416729

Chain	Residue	Details
A	ALA1-TYR222
E	ARG271-LYS281
A	ARG271-LYS281
B	ALA1-TYR222
B	ARG271-LYS281
C	ALA1-TYR222
C	ARG271-LYS281
D	ALA1-TYR222
D	ARG271-LYS281
E	ALA1-TYR222

site_id	SWS_FT_FI2
Number of Residues	105
Details	TRANSMEM: Helical; Name=1 => ECO:0000269\|PubMed:26416729

Chain	Residue	Details
A	TYR223-ILE244
B	TYR223-ILE244
C	TYR223-ILE244
D	TYR223-ILE244
E	TYR223-ILE244

site_id	SWS_FT_FI3
Number of Residues	20
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:26416729

Chain	Residue	Details
A	ASN245-ALA249
B	ASN245-ALA249
C	ASN245-ALA249
D	ASN245-ALA249
E	ASN245-ALA249

site_id	SWS_FT_FI4
Number of Residues	100
Details	TRANSMEM: Helical; Name=2 => ECO:0000269\|PubMed:26416729

Chain	Residue	Details
A	PRO250-SER270
B	PRO250-SER270
C	PRO250-SER270
D	PRO250-SER270
E	PRO250-SER270

site_id	SWS_FT_FI5
Number of Residues	100
Details	TRANSMEM: Helical; Name=3 => ECO:0000269\|PubMed:26416729

Chain	Residue	Details
A	ALA282-ALA302
B	ALA282-ALA302
C	ALA282-ALA302
D	ALA282-ALA302
E	ALA282-ALA302

site_id	SWS_FT_FI6
Number of Residues	100
Details	TRANSMEM: Helical; Name=4 => ECO:0000269\|PubMed:26416729

Chain	Residue	Details
A	ILE325-TYR345
B	ILE325-TYR345
C	ILE325-TYR345
D	ILE325-TYR345
E	ILE325-TYR345

site_id	SWS_FT_FI7
Number of Residues	15
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P23415

Chain	Residue	Details
A	GLU192
D	GLU192
D	ASP194
D	HIS215
E	GLU192
E	ASP194
E	HIS215
A	ASP194
A	HIS215
B	GLU192
B	ASP194
B	HIS215
C	GLU192
C	ASP194
C	HIS215

site_id	SWS_FT_FI8
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:26416729

Chain	Residue	Details
A	TYR202
B	TYR202
C	TYR202
D	TYR202
E	TYR202

site_id	SWS_FT_FI9
Number of Residues	5
Details	SITE: Important for obstruction of the ion pore in the closed conformation => ECO:0000269\|PubMed:26416729

Chain	Residue	Details
A	LEU261
B	LEU261
C	LEU261
D	LEU261
E	LEU261

site_id	SWS_FT_FI10
Number of Residues	5
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269\|PubMed:26416729, ECO:0007744\|PDB:5CFB

Chain	Residue	Details
A	GLN38
B	GLN38
C	GLN38
D	GLN38
E	GLN38

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