4X5T

alpha 1 glycine receptor transmembrane structure fused to the extracellular domain of GLIC

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	0006811	biological_process	monoatomic ion transport
A	0016020	cellular_component	membrane
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	0006811	biological_process	monoatomic ion transport
B	0016020	cellular_component	membrane
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	0006811	biological_process	monoatomic ion transport
C	0016020	cellular_component	membrane
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	0006811	biological_process	monoatomic ion transport
D	0016020	cellular_component	membrane
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	0006811	biological_process	monoatomic ion transport
E	0016020	cellular_component	membrane
E	0034220	biological_process	monoatomic ion transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue NI A 501

Chain	Residue
A	ASP86
A	ALA87
A	ASP88

---

site_id	AC2
Number of Residues	2
Details	binding site for residue CL A 502

Chain	Residue
A	PHE78
A	ARG85

---

site_id	AC3
Number of Residues	5
Details	binding site for residue ACT A 503

Chain	Residue
E	ARG105
A	ARG77
A	ILE131
A	GLU181
E	PHE42

---

site_id	AC4
Number of Residues	3
Details	binding site for residue NI B 501

Chain	Residue
B	ASP86
B	ALA87
B	ASP88

---

site_id	AC5
Number of Residues	3
Details	binding site for residue CL B 502

Chain	Residue
B	PRO74
B	ILE76
B	ARG85

---

site_id	AC6
Number of Residues	2
Details	binding site for residue CL B 503

Chain	Residue
B	PHE78
B	ARG85

---

site_id	AC7
Number of Residues	5
Details	binding site for residue ACT B 504

Chain	Residue
A	PHE42
A	ARG105
B	ARG77
B	ILE131
B	GLU181

---

site_id	AC8
Number of Residues	3
Details	binding site for residue NI C 501

Chain	Residue
C	ASP86
C	ALA87
C	ASP88

---

site_id	AC9
Number of Residues	2
Details	binding site for residue CL C 502

Chain	Residue
C	PHE78
C	ARG85

---

site_id	AD1
Number of Residues	3
Details	binding site for residue CL C 503

Chain	Residue
C	PRO74
C	ILE76
C	ARG85

---

site_id	AD2
Number of Residues	5
Details	binding site for residue ACT C 504

Chain	Residue
B	PHE42
B	ARG105
C	ARG77
C	ILE131
C	GLU181

---

site_id	AD3
Number of Residues	2
Details	binding site for residue NI D 501

Chain	Residue
D	PRO74
D	ARG85

---

site_id	AD4
Number of Residues	3
Details	binding site for residue NI D 502

Chain	Residue
D	ASP86
D	ALA87
D	ASP88

---

site_id	AD5
Number of Residues	5
Details	binding site for residue ACT D 503

Chain	Residue
C	PHE42
C	ARG105
D	ARG77
D	ILE131
D	GLU181

---

site_id	AD6
Number of Residues	3
Details	binding site for residue NI E 501

Chain	Residue
E	ASP86
E	ALA87
E	ASP88

---

site_id	AD7
Number of Residues	2
Details	binding site for residue CL E 502

Chain	Residue
E	PHE78
E	ARG85

---

site_id	AD8
Number of Residues	5
Details	binding site for residue ACT E 503

Chain	Residue
D	PHE42
D	ARG105
E	ARG77
E	ILE131
E	GLU181

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	955
Details	TOPO_DOM: Periplasmic => ECO:0000255

Chain	Residue	Details
A	GLN2-GLN219
B	GLN2-GLN219
C	GLN2-GLN219
D	GLN2-GLN219
E	GLN2-GLN219

---

site_id	SWS_FT_FI2
Number of Residues	105
Details	TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:23994010, ECO:0000269|PubMed:25730860

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:23994010, ECO:0000269|PubMed:25730860

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:23994010, ECO:0000269|PubMed:25730860

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	50
Details	TOPO_DOM: Extracellular => ECO:0000269|PubMed:23994010, ECO:0000269|PubMed:25730860

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

---

site_id	SWS_FT_FI6
Number of Residues	100
Details	TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:23994010, ECO:0000269|PubMed:25730860

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

---

site_id	SWS_FT_FI7
Number of Residues	100
Details	TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:23994010

Chain	Residue	Details
A	ILE390-TYR410
B	ILE390-TYR410
C	ILE390-TYR410
D	ILE390-TYR410
E	ILE390-TYR410

---

site_id	SWS_FT_FI8
Number of Residues	5
Details	SITE: Important for obstruction of the ion pore in the closed conformation => ECO:0000269|PubMed:25730860

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

---