Structure of PDB 4hfp Chain D

Receptor sequence
>4hfpD (length=257) Species: 9606 (Homo sapiens) [Search protein sequence]
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTA
NVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDA
CEGDAGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWI
QKVIDQF
3D structure
PDB4hfp Autoactivation of thrombin precursors.
ChainD
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 E192 G193 D194 A195 G196
Catalytic site (residue number reindexed from 1) H43 D99 E202 G203 D204 A205 G206
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 D E127 Y134 P204 F204A E124 Y134 P214 F215
BS02 15U D H57 Y60A W60D A190 E192 W215 G216 H43 Y47 W50 A200 E202 W227 G228 MOAD: Kd=42nM
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005509 calcium ion binding
Biological Process
GO:0006508 proteolysis
GO:0007596 blood coagulation

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Molecular Function
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Biological Process
External links
PDB RCSB:4hfp, PDBe:4hfp, PDBj:4hfp
PDBsum4hfp
PubMed23467412
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

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