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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3VW7

Crystal structure of human protease-activated receptor 1 (PAR1) bound with antagonist vorapaxar at 2.2 angstrom

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0003824	molecular_function	catalytic 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	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0030430	cellular_component	host cell cytoplasm
A	0031640	biological_process	killing of cells of another organism
A	0042742	biological_process	defense response to bacterium
A	0044659	biological_process	viral release from host cell by cytolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE VPX A 2001

Chain	Residue
A	TYR183
A	LEU332
A	LEU333
A	TYR337
A	ALA349
A	TYR350
A	TYR353
A	HOH3004
A	TYR187
A	PRO236
A	HIS255
A	ASP256
A	VAL257
A	LEU258
A	PHE271
A	ARG1080

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OLC A 2002

Chain	Residue
A	PHE157
A	TYR206
A	ILE284
A	ARG295
A	OLC2003

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC A 2003

Chain	Residue
A	SER160
A	SER164
A	OLC2002
A	OLC2004

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OLC A 2004

Chain	Residue
A	PHE113
A	PRO156
A	SER160
A	PHE163
A	SER164
A	LEU202
A	LEU229
A	PHE278
A	OLC2003
A	OLC2010

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE OLC A 2005

Chain	Residue
A	MET122
A	VAL126
A	PHE127
A	CYS365
A	PRO368
A	TYR371
A	TYR372
A	SER375

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OLC A 2006

Chain	Residue
A	TRP100
A	PRO328
A	ALA348
A	PHE351
A	CYS356
A	HOH3067

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OLC A 2007

Chain	Residue
A	GLY327
A	PRO328
A	THR343
A	THR346
A	ALA348
A	CYS356

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OLC A 2008

Chain	Residue
A	VAL139
A	HIS143
A	SER220
A	LEU224
A	ALA228

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC A 2009

Chain	Residue
A	PRO236
A	LYS240
A	TYR270
A	PHE271

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC A 2010

Chain	Residue
A	PHE163
A	PHE221
A	THR222
A	OLC2004

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 2011

Chain	Residue
A	LYS135
A	LYS307

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 2012

Chain	Residue
A	LEU144
A	ASP148
A	SER189
A	ASP367
A	HOH3065
A	HOH3066

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. ASIlLMTVISIDRFLaV

Chain	Residue	Details
A	ALA188-VAL204

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	25
Details	TRANSMEM: Helical; Name=1 => ECO:0000255

Chain	Residue	Details
A	LEU103-ILE128

site_id	SWS_FT_FI2
Number of Residues	27
Details	TOPO_DOM: Cytoplasmic => ECO:0000255

Chain	Residue	Details
A	LEU129-ALA137
A	ASP199-ARG218

site_id	SWS_FT_FI3
Number of Residues	19
Details	TRANSMEM: Helical; Name=2 => ECO:0000255

Chain	Residue	Details
A	VAL138-PHE157

site_id	SWS_FT_FI4
Number of Residues	61
Details	TOPO_DOM: Extracellular => ECO:0000255

Chain	Residue	Details
A	LYS158-ARG176
A	LYS240-ALA268
A	ALA335-TYR350

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

Chain	Residue	Details
A	PHE177-ILE198

site_id	SWS_FT_FI6
Number of Residues	20
Details	TRANSMEM: Helical; Name=4 => ECO:0000255

Chain	Residue	Details
A	ALA219-LEU239

site_id	SWS_FT_FI7
Number of Residues	19
Details	TRANSMEM: Helical; Name=5 => ECO:0000255

Chain	Residue	Details
A	TYR269-VAL288

site_id	SWS_FT_FI8
Number of Residues	22
Details	TRANSMEM: Helical; Name=6 => ECO:0000255

Chain	Residue	Details
A	LEU312-ILE334

site_id	SWS_FT_FI9
Number of Residues	23
Details	TRANSMEM: Helical; Name=7 => ECO:0000255

Chain	Residue	Details
A	PHE351-ALA374

site_id	SWS_FT_FI10
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	GLY250
A	SER259

site_id	SWS_FT_FI11
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_04110, ECO:0000269\|PubMed:3382407, ECO:0000269\|PubMed:7831309, ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	GLU1011

site_id	SWS_FT_FI12
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_04110, ECO:0000269\|PubMed:1892846, ECO:0000269\|PubMed:3382407, ECO:0000269\|PubMed:7831309, ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	ASN1020

site_id	SWS_FT_FI13
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	LEU1032
A	PHE1104

site_id	SWS_FT_FI14
Number of Residues	2
Details	BINDING: BINDING => ECO:0000303\|PubMed:7831309

Chain	Residue	Details
A	SER1117
A	ASN1132

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU1011	proton shuttle (general acid/base)
A	ASN1020	covalent catalysis

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PDB entries from 2025-06-18

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