4ISH

Structure of FACTOR VIIA in complex with the inhibitor BMS-593214 also known as 2'-[(6R,6AR,11BR)-2-CARBAMIMIDOYL-6,6A,7,11B-TETRAHYDRO-5H-INDENO[2,1-C]QUINOLIN-6-YL]-5'-HYDROXY-4'-METHOXYBIPHENYL-4-CARBOXYLIC ACID

Functional Information from GO Data

Chain	GOid	namespace	contents
H	0004252	molecular_function	serine-type endopeptidase activity
H	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 1GE H 301

Chain	Residue
H	HIS57
H	TRP215
H	GLY216
H	GLY219
H	GLY226
H	HOH413
H	HOH422
H	HOH512
H	HOH565
H	THR98
H	ASP102
H	ASP189
H	SER190
H	CYS191
H	LYS192
H	SER195
H	SER214

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA H 302

Chain	Residue
H	GLU70
H	ASP72
H	GLU75
H	GLU80
H	HOH448
H	HOH579

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Functional Information from PROSITE/UniProt

site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC

Chain	Residue	Details
H	VAL53-CYS58

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site_id	PS00135
Number of Residues	12
Details	TRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGPHA

Chain	Residue	Details
H	ASP189-ALA200

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site_id	PS01186
Number of Residues	16
Details	EGF_2 EGF-like domain signature 2. CrCheGYslladgvsC

Chain	Residue	Details
L	CYS112-CYS127

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Charge relay system => ECO:0000250

Chain	Residue	Details
H	HIS57
H	ASP102
H	SER195

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
H	ASP189

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725

Chain	Residue	Details
H	ASN175

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