Structure of PDB 4hfp Chain B

Receptor sequence
>4hfpB (length=257) Species: 9606 (Homo sapiens) [Search protein sequence]
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTA
NVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDA
CEGDAGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWI
QKVIDQF
3D structure
PDB4hfp Autoactivation of thrombin precursors.
ChainB
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 B E23 M26 P28 W29 D116 H119 P120 V121 C122 Y134 K135 G136 R137 N159 K202 N205 R206 W207 E8 M11 P13 W14 D113 H116 P117 V118 C119 Y134 K135 G136 R137 N164 K212 N217 R218 W219
BS02 15U B H57 W60D D189 A190 E192 W215 G216 H43 W50 D199 A200 E202 W227 G228 MOAD: Kd=42nM
PDBbind-CN: -logKd/Ki=7.38,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

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

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