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
PDB1bcu X-ray and spectrophotometric studies of the binding of proflavin to the S1 specificity pocket of human alpha-thrombin.
ChainH
Resolution2.0 Å
3D
structure
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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
External links
PDB RCSB:1bcu, PDBe:1bcu, PDBj:1bcu
PDBsum1bcu
PubMed9559654
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

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