1HUT

THE STRUCTURE OF ALPHA-THROMBIN INHIBITED BY A 15-MER SINGLE-STRANDED DNA APTAMER

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
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 PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 0G7 H 1

Chain	Residue
H	HIS57
H	SER195
H	SER214
H	TRP215
H	GLY216
H	CYS220
H	TYR60
H	TRP60
H	ASN98
H	LEU99
H	ILE174
H	ASP189
H	ALA190
H	CYS191

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site_id	CAT
Number of Residues	3
Details	CATALYTIC SITE

Chain	Residue
H	HIS57
H	ASP102
H	SER195

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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. LTAAHC

Chain	Residue	Details
H	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
H	ASP189-VAL200

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Charge relay system

Chain	Residue	Details
H	HIS57
H	ASP102
H	SER195

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site_id	SWS_FT_FI2
Number of Residues	1
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
H	ASN60

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