Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6PLR

CryoEM structure of zebra fish alpha-1 glycine receptor bound with glycine in nanodisc, desensitized state

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	0006821	biological_process	chloride transport
A	0016020	cellular_component	membrane
A	0016594	molecular_function	glycine binding
A	0016934	molecular_function	extracellularly glycine-gated chloride channel activity
A	0022824	molecular_function	transmitter-gated monoatomic ion channel activity
A	0034220	biological_process	monoatomic ion transmembrane transport
A	0045211	cellular_component	postsynaptic membrane
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	0006821	biological_process	chloride transport
B	0016020	cellular_component	membrane
B	0016594	molecular_function	glycine binding
B	0016934	molecular_function	extracellularly glycine-gated chloride channel activity
B	0022824	molecular_function	transmitter-gated monoatomic ion channel activity
B	0034220	biological_process	monoatomic ion transmembrane transport
B	0045211	cellular_component	postsynaptic membrane
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	0006821	biological_process	chloride transport
C	0016020	cellular_component	membrane
C	0016594	molecular_function	glycine binding
C	0016934	molecular_function	extracellularly glycine-gated chloride channel activity
C	0022824	molecular_function	transmitter-gated monoatomic ion channel activity
C	0034220	biological_process	monoatomic ion transmembrane transport
C	0045211	cellular_component	postsynaptic membrane
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	0006821	biological_process	chloride transport
D	0016020	cellular_component	membrane
D	0016594	molecular_function	glycine binding
D	0016934	molecular_function	extracellularly glycine-gated chloride channel activity
D	0022824	molecular_function	transmitter-gated monoatomic ion channel activity
D	0034220	biological_process	monoatomic ion transmembrane transport
D	0045211	cellular_component	postsynaptic membrane
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	0006821	biological_process	chloride transport
E	0016020	cellular_component	membrane
E	0016594	molecular_function	glycine binding
E	0016934	molecular_function	extracellularly glycine-gated chloride channel activity
E	0022824	molecular_function	transmitter-gated monoatomic ion channel activity
E	0034220	biological_process	monoatomic ion transmembrane transport
E	0045211	cellular_component	postsynaptic membrane

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	CYS154-CYS168

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1205
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:26344198

Chain	Residue	Details
A	ALA17-TYR238
D	ALA17-TYR238
D	ARG287-LYS297
D	LYS426-GLN436
E	ALA17-TYR238
E	ARG287-LYS297
E	LYS426-GLN436
A	ARG287-LYS297
A	LYS426-GLN436
B	ALA17-TYR238
B	ARG287-LYS297
B	LYS426-GLN436
C	ALA17-TYR238
C	ARG287-LYS297
C	LYS426-GLN436

site_id	SWS_FT_FI2
Number of Residues	105
Details	TRANSMEM: Helical; Name=1 => ECO:0000269\|PubMed:26344198

Chain	Residue	Details
A	TYR239-ILE260
B	TYR239-ILE260
C	TYR239-ILE260
D	TYR239-ILE260
E	TYR239-ILE260

site_id	SWS_FT_FI3
Number of Residues	445
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:26344198

Chain	Residue	Details
A	ASN261-ALA265
E	ALA319-THR404
A	ALA319-THR404
B	ASN261-ALA265
B	ALA319-THR404
C	ASN261-ALA265
C	ALA319-THR404
D	ASN261-ALA265
D	ALA319-THR404
E	ASN261-ALA265

site_id	SWS_FT_FI4
Number of Residues	100
Details	TRANSMEM: Helical; Name=2 => ECO:0000269\|PubMed:26344198

Chain	Residue	Details
A	PRO266-SER286
B	PRO266-SER286
C	PRO266-SER286
D	PRO266-SER286
E	PRO266-SER286

site_id	SWS_FT_FI5
Number of Residues	100
Details	TRANSMEM: Helical; Name=3 => ECO:0000269\|PubMed:26344198

Chain	Residue	Details
A	ALA298-ALA318
B	ALA298-ALA318
C	ALA298-ALA318
D	ALA298-ALA318
E	ALA298-ALA318

site_id	SWS_FT_FI6
Number of Residues	100
Details	TRANSMEM: Helical; Name=4 => ECO:0000269\|PubMed:26344198

Chain	Residue	Details
A	VAL405-TYR425
B	VAL405-TYR425
C	VAL405-TYR425
D	VAL405-TYR425
E	VAL405-TYR425

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

Chain	Residue	Details
A	GLU208
D	GLU208
D	ASP210
D	HIS231
E	GLU208
E	ASP210
E	HIS231
A	ASP210
A	HIS231
B	GLU208
B	ASP210
B	HIS231
C	GLU208
C	ASP210
C	HIS231

site_id	SWS_FT_FI8
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:26344198

Chain	Residue	Details
A	TYR218
B	TYR218
C	TYR218
D	TYR218
E	TYR218

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:26344198

Chain	Residue	Details
A	LEU277
B	LEU277
C	LEU277
D	LEU277
E	LEU277

site_id	SWS_FT_FI10
Number of Residues	5
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269\|PubMed:26344198

Chain	Residue	Details
A	ASN54
B	ASN54
C	ASN54
D	ASN54
E	ASN54

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)