Structure of PDB 1afe Chain H

Receptor sequence
>1afeH (length=253) Species: 9606 (Homo sapiens) [Search protein sequence]
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWGQ
PSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSG
GPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQ
FGE
3D structure
PDB1afe Human alpha-thrombin inhibition by the highly selective compounds N-ethoxycarbonyl-D-Phe-Pro-alpha-azaLys p-nitrophenyl ester and N-carbobenzoxy-Pro-alpha-azaLys p-nitrophenyl ester: a kinetic, thermodynamic and X-ray crystallographic study.
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 F34 R67 R73 T74 R75 Y76 I82 M84 F19 R62 R68 T69 R70 Y71 I78 M80
BS02 ALZ H H57 Y60A I174 D189 A190 C191 S195 W215 G216 E217 G219 H43 Y47 I173 D193 A194 C195 S199 W221 G222 E223 G224
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:1afe, PDBe:1afe, PDBj:1afe
PDBsum1afe
PubMed9217260
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

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