6IGL

Crystal Structure of human ETB receptor in complex with IRL1620

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0004930	molecular_function	G protein-coupled receptor activity
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0009253	biological_process	peptidoglycan catabolic process
A	0016020	cellular_component	membrane
A	0016998	biological_process	cell wall macromolecule catabolic process
B	0005576	cellular_component	extracellular region
B	0019229	biological_process	regulation of vasoconstriction

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue CIT A 1201

Chain	Residue
A	ARG1006
A	GLY1111
A	PHE1112
A	THR1113
A	ASN1114
A	SER1115
A	ASN1130
A	HOH1307
A	HOH1333

---

site_id	AC2
Number of Residues	7
Details	binding site for residue SO4 A 1202

Chain	Residue
A	LYS303
A	HIS314
A	GLU1003
A	ARG1006
A	LYS1058
A	GLU1062
A	HOH1301

---

site_id	AC3
Number of Residues	7
Details	binding site for residue SO4 A 1203

Chain	Residue
A	GLY1049
A	ARG1050
A	LYS1058
A	ASP1059
A	LYS1133
A	HOH1303
A	HOH1327

---

site_id	AC4
Number of Residues	4
Details	binding site for residue SO4 A 1204

Chain	Residue
A	THR1140
A	PRO1141
A	ASN1142
A	ARG1143

---

site_id	AC5
Number of Residues	3
Details	binding site for residue SO4 A 1205

Chain	Residue
A	SER1036
A	LEU1037
A	ASN1038

---

site_id	AC6
Number of Residues	2
Details	binding site for residue OLC A 1206

Chain	Residue
A	TYR200
A	ARG201

---

site_id	AC7
Number of Residues	8
Details	binding site for residue OLC A 1207

Chain	Residue
A	SER1036
A	ASN1038
A	LYS1122
A	ARG1123
A	TRP1124
A	ASP1125
A	GLU1126
A	OLC1208

---

site_id	AC8
Number of Residues	6
Details	binding site for residue OLC A 1208

Chain	Residue
A	ARG319
A	LYS323
A	ARG1152
A	THR1153
A	THR1155
A	OLC1207

---

Functional Information from PROSITE/UniProt

site_id	PS00237
Number of Residues	17
Details	G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ITVlSLCALSIDRYRaV

Chain	Residue	Details
A	ILE187-VAL203

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	TRANSMEM: Helical; Name=1 => ECO:0000255

Chain	Residue	Details
A	TYR102-ILE126

---

site_id	SWS_FT_FI2
Number of Residues	30
Details	TOPO_DOM: Cytoplasmic => ECO:0000255

Chain	Residue	Details
A	TYR127-ASN137
A	ASP198-THR218

---

site_id	SWS_FT_FI3
Number of Residues	25
Details	TRANSMEM: Helical; Name=2 => ECO:0000255

Chain	Residue	Details
A	ILE138-LEU163

---

site_id	SWS_FT_FI4
Number of Residues	49
Details	TOPO_DOM: Extracellular => ECO:0000255

Chain	Residue	Details
A	ALA164-LYS175
A	THR244-THR271
A	ASN351-SER362

---

site_id	SWS_FT_FI5
Number of Residues	21
Details	TRANSMEM: Helical; Name=3 => ECO:0000255

Chain	Residue	Details
A	LEU176-ILE197

---

site_id	SWS_FT_FI6
Number of Residues	24
Details	TRANSMEM: Helical; Name=4 => ECO:0000255

Chain	Residue	Details
A	ALA219-ILE243

---

site_id	SWS_FT_FI7
Number of Residues	24
Details	TRANSMEM: Helical; Name=5 => ECO:0000255

Chain	Residue	Details
A	ALA272-MET296

---

site_id	SWS_FT_FI8
Number of Residues	25
Details	TRANSMEM: Helical; Name=6 => ECO:0000255

Chain	Residue	Details
A	VAL325-TYR350

---

site_id	SWS_FT_FI9
Number of Residues	26
Details	TRANSMEM: Helical; Name=7 => ECO:0000255

Chain	Residue	Details
A	PHE363-VAL389

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P28088

Chain	Residue	Details
A	SER1042

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:9261180

Chain	Residue	Details
A	CYS402

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	LIPID: S-palmitoyl cysteine => ECO:0000255

Chain	Residue	Details
A	CYS403
A	ALA405

---