3B9F

1.6 A structure of the PCI-thrombin-heparin complex

Functional Information from GO Data

Chain	GOid	namespace	contents
H	0004252	molecular_function	serine-type endopeptidase activity
H	0005509	molecular_function	calcium ion binding
H	0006508	biological_process	proteolysis
H	0007596	biological_process	blood coagulation
I	0001972	molecular_function	retinoic acid binding
I	0002080	cellular_component	acrosomal membrane
I	0004867	molecular_function	serine-type endopeptidase inhibitor activity
I	0005576	cellular_component	extracellular region
I	0005615	cellular_component	extracellular space
I	0006869	biological_process	lipid transport
I	0007338	biological_process	single fertilization
I	0008201	molecular_function	heparin binding
I	0031091	cellular_component	platelet alpha granule
I	0031094	cellular_component	platelet dense tubular network
I	0031210	molecular_function	phosphatidylcholine binding
I	0036024	cellular_component	protein C inhibitor-TMPRSS7 complex
I	0036025	cellular_component	protein C inhibitor-TMPRSS11E complex
I	0036026	cellular_component	protein C inhibitor-PLAT complex
I	0036027	cellular_component	protein C inhibitor-PLAU complex
I	0036028	cellular_component	protein C inhibitor-thrombin complex
I	0036029	cellular_component	protein C inhibitor-KLK3 complex
I	0036030	cellular_component	protein C inhibitor-plasma kallikrein complex
I	0097181	cellular_component	protein C inhibitor-coagulation factor V complex
I	0097182	cellular_component	protein C inhibitor-coagulation factor Xa complex
I	0097183	cellular_component	protein C inhibitor-coagulation factor XI complex
L	0004252	molecular_function	serine-type endopeptidase activity
L	0005576	cellular_component	extracellular region
L	0006508	biological_process	proteolysis
L	0007596	biological_process	blood coagulation

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
H	LEU53-CYS58

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site_id	PS00284
Number of Residues	11
Details	SERPIN Serpins signature. LVFNRPFLMfI

Chain	Residue	Details
I	LEU363-ILE373

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	SITE: Reactive bond

Chain	Residue	Details
I	ARG354
H	ASP102
H	ALA195

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site_id	SWS_FT_FI2
Number of Residues	2
Details	CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:19674964

Chain	Residue	Details
I	THR20
I	VAL21

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site_id	SWS_FT_FI3
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
I	ASN230
I	ASN243
I	ASN319

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
H	ASP102
H	ALA195
H	GLY193
H	HIS57

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
H	ASP102
H	HIS57

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site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
H	ASP102
H	ALA195
H	HIS57

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site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
H	ALA195
H	GLY193

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site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
H	ALA195
H	GLY196

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