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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4XNV

The human P2Y1 receptor in complex with BPTU

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004930	molecular_function	G protein-coupled receptor activity
A	0005506	molecular_function	iron ion binding
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0007200	biological_process	phospholipase C-activating G protein-coupled receptor signaling pathway
A	0009055	molecular_function	electron transfer activity
A	0016020	cellular_component	membrane
A	0030168	biological_process	platelet activation
A	0043448	biological_process	alkane catabolic process
A	0045028	molecular_function	G protein-coupled purinergic nucleotide receptor activity
A	0046872	molecular_function	metal ion binding
A	0090075	biological_process	relaxation of muscle

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue BUR A 1101

Chain	Residue
A	PHE62
A	OLC1107
A	OLC1110
A	OLC1113
A	1PE1114
A	PHE66
A	LEU102
A	THR103
A	PRO105
A	ALA106
A	MET123
A	GLN127
A	Y011105

site_id	AC2
Number of Residues	5
Details	binding site for residue CLR A 1102

Chain	Residue
A	PRO185
A	TYR189
A	SER213
A	TYR217
A	Y011103

site_id	AC3
Number of Residues	8
Details	binding site for residue Y01 A 1103

Chain	Residue
A	ILE216
A	CYS220
A	ALA270
A	MET279
A	ARG301
A	THR305
A	CLR1102
A	1PE1114

site_id	AC4
Number of Residues	7
Details	binding site for residue Y01 A 1104

Chain	Residue
A	TYR89
A	CYS144
A	HIS148
A	ALA224
A	LEU232
A	TYR246
A	LEU266

site_id	AC5
Number of Residues	9
Details	binding site for residue Y01 A 1105

Chain	Residue
A	PHE62
A	ILE108
A	PHE109
A	PHE112
A	ASN113
A	ARG301
A	BUR1101
A	OLC1113
A	1PE1114

site_id	AC6
Number of Residues	5
Details	binding site for residue OLC A 1106

Chain	Residue
A	ARG212
A	PHE215
A	ILE216
A	ASP289
A	OLC1112

site_id	AC7
Number of Residues	9
Details	binding site for residue OLC A 1107

Chain	Residue
A	PHE109
A	SER184
A	PHE188
A	TYR189
A	TYR210
A	SER213
A	ARG301
A	BUR1101
A	1PE1114

site_id	AC8
Number of Residues	4
Details	binding site for residue OLC A 1108

Chain	Residue
A	ASP121
A	PHE129
A	OLC1110
A	HOH1206

site_id	AC9
Number of Residues	6
Details	binding site for residue OLC A 1109

Chain	Residue
A	LYS46
A	PHE49
A	TYR53
A	PHE112
A	CYS318
A	OLC1111

site_id	AD1
Number of Residues	10
Details	binding site for residue OLC A 1110

Chain	Residue
A	ILE118
A	PHE119
A	ASP121
A	MET123
A	LYS125
A	SER184
A	LEU187
A	PHE188
A	BUR1101
A	OLC1108

site_id	AD2
Number of Residues	6
Details	binding site for residue OLC A 1111

Chain	Residue
A	PHE51
A	TYR52
A	PRO55
A	TYR111
A	PHE112
A	OLC1109

site_id	AD3
Number of Residues	5
Details	binding site for residue OLC A 1112

Chain	Residue
A	PHE226
A	THR281
A	MET282
A	ARG285
A	OLC1106

site_id	AD4
Number of Residues	9
Details	binding site for residue OLC A 1113

Chain	Residue
A	THR267
A	ALA270
A	ARG301
A	THR305
A	VAL308
A	BUR1101
A	Y011105
A	1PE1114
A	HOH1217

site_id	AD5
Number of Residues	6
Details	binding site for residue 1PE A 1114

Chain	Residue
A	Y011105
A	OLC1107
A	OLC1113
A	ARG301
A	BUR1101
A	Y011103

site_id	AD6
Number of Residues	4
Details	binding site for residue ZN A 1115

Chain	Residue
A	CYS1006
A	CYS1009
A	CYS1039
A	CYS1042

Functional Information from PROSITE/UniProt

site_id	PS00202
Number of Residues	11
Details	RUBREDOXIN Rubredoxin signature. IpDDWvCPlCG

Chain	Residue	Details
A	ILE1033-GLY1043

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

Chain	Residue	Details
A	GLY137-VAL153

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	22
Details	TRANSMEM: Helical; Name=1 => ECO:0000269\|PubMed:25822790

Chain	Residue	Details
A	TYR52-TRP74

site_id	SWS_FT_FI2
Number of Residues	77
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:25822790

Chain	Residue	Details
A	MET75-SER87
A	HIS148-LYS166
A	LEU326-LEU373

site_id	SWS_FT_FI3
Number of Residues	21
Details	TRANSMEM: Helical; Name=2 => ECO:0000269\|PubMed:25822790

Chain	Residue	Details
A	VAL88-PHE109

site_id	SWS_FT_FI4
Number of Residues	58
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:25822790

Chain	Residue	Details
A	TYR110-LYS125
A	TYR189-TYR214
A	ARG285-TYR303

site_id	SWS_FT_FI5
Number of Residues	21
Details	TRANSMEM: Helical; Name=3 => ECO:0000269\|PubMed:25822790

Chain	Residue	Details
A	LEU126-ALA147

site_id	SWS_FT_FI6
Number of Residues	21
Details	TRANSMEM: Helical; Name=4 => ECO:0000269\|PubMed:25822790

Chain	Residue	Details
A	ASN167-PHE188

site_id	SWS_FT_FI7
Number of Residues	22
Details	TRANSMEM: Helical; Name=5 => ECO:0000269\|PubMed:25822790

Chain	Residue	Details
A	PHE215-TYR237

site_id	SWS_FT_FI8
Number of Residues	23
Details	TRANSMEM: Helical; Name=6 => ECO:0000269\|PubMed:25822790

Chain	Residue	Details
A	LEU261-LEU284

site_id	SWS_FT_FI9
Number of Residues	21
Details	TRANSMEM: Helical; Name=7 => ECO:0000269\|PubMed:25822790

Chain	Residue	Details
A	ALA304-PHE325

site_id	SWS_FT_FI10
Number of Residues	5
Details	BINDING: BINDING => ECO:0000305\|PubMed:25822790, ECO:0007744\|PDB:4XNW

Chain	Residue	Details
A	LYS46
A	TYR203
A	ASN283
A	TYR303
A	ARG310

site_id	SWS_FT_FI11
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN11
A	ASN27
A	ASN113
A	ASN197

site_id	SWS_FT_FI12
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00241, ECO:0000269\|PubMed:10216292

Chain	Residue	Details
A	CYS1006
A	CYS1009
A	CYS1039
A	CYS1042

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: N-formylmethionine => ECO:0000269\|PubMed:1637309

Chain	Residue	Details
A	MET1001

225158

PDB entries from 2024-09-18

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