1E0F

Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005576	cellular_component	extracellular region
A	0006508	biological_process	proteolysis
A	0007596	biological_process	blood coagulation
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005576	cellular_component	extracellular region
B	0006508	biological_process	proteolysis
B	0007596	biological_process	blood coagulation
C	0004252	molecular_function	serine-type endopeptidase activity
C	0005576	cellular_component	extracellular region
C	0006508	biological_process	proteolysis
C	0007596	biological_process	blood coagulation
D	0004252	molecular_function	serine-type endopeptidase activity
D	0005509	molecular_function	calcium ion binding
D	0006508	biological_process	proteolysis
D	0007596	biological_process	blood coagulation
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005509	molecular_function	calcium ion binding
E	0006508	biological_process	proteolysis
E	0007596	biological_process	blood coagulation
F	0004252	molecular_function	serine-type endopeptidase activity
F	0005509	molecular_function	calcium ion binding
F	0006508	biological_process	proteolysis
F	0007596	biological_process	blood coagulation
I	0004857	molecular_function	enzyme inhibitor activity
I	0004867	molecular_function	serine-type endopeptidase inhibitor activity
I	0030414	molecular_function	peptidase inhibitor activity
J	0004857	molecular_function	enzyme inhibitor activity
J	0004867	molecular_function	serine-type endopeptidase inhibitor activity
J	0030414	molecular_function	peptidase inhibitor activity
K	0004857	molecular_function	enzyme inhibitor activity
K	0004867	molecular_function	serine-type endopeptidase inhibitor activity
K	0030414	molecular_function	peptidase inhibitor activity

Functional Information from PROSITE/UniProt

site_id	PS00010
Number of Residues	12
Details	ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CpDgevgYtCdC

Chain	Residue	Details
I	CYS10-CYS21

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

Chain	Residue	Details
D	LEU53-CYS58

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

Chain	Residue	Details
D	ASP189-VAL200

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	ACT_SITE: Charge relay system

Chain	Residue	Details
D	HIS57
D	ASP102
D	SER195
E	HIS57
E	ASP102
E	SER195
F	HIS57
F	ASP102
F	SER195

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site_id	SWS_FT_FI2
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923

Chain	Residue	Details
D	ASN60
E	ASN60
F	ASN60

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