BioLiP

Structure of PDB 1bcu Chain H

Receptor sequence

>1bcuH (length=249) Species: 9606 (Homo sapiens) [Search protein sequence]

IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKEGQPS
VLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGP
FVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQF

3D structure

PDB

1bcu X-ray and spectrophotometric studies of the binding of proflavin to the S1 specificity pocket of human alpha-thrombin.

Chain

Resolution

2.0 Å

3D
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Enzymatic activity

Enzyme Commision number

3.4.21.5: thrombin.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	peptide	H	E23 G25 M26 P28 W29 H119 P120 C122 Y134 K135 R137 N159 M201 K202 P204 N205 R206 W207	E8 G10 M11 P13 W14 H116 P117 C119 Y134 K135 R137 N156 M203 K204 P206 N209 R210 W211
BS02	peptide	H	F34 L40 L65 R73 T74 R75 Y76 K81 I82	F19 L26 L60 R68 T69 R70 Y71 K77 I78
BS03	PRL	H	D189 A190 W215 G216 G219 C220	D191 A192 W219 G220 G222 C223	MOAD: Kd=0.53mM PDBbind-CN: -logKd/Ki=3.28,Kd=0.53mM BindingDB: IC50=12000nM

Gene Ontology

	Molecular Function
GO:0004252	serine-type endopeptidase activity
GO:0005509	calcium ion binding

	Biological Process
GO:0006508	proteolysis
GO:0007596	blood coagulation

View graph for
Molecular Function

View graph for
Biological Process

PDB	RCSB:1bcu, PDBe:1bcu, PDBj:1bcu
PDBsum	1bcu
PubMed	9559654
UniProt	P00734\|THRB_HUMAN Prothrombin (Gene Name=F2)