Structure of PDB 3pmh Chain B

Receptor sequence
>3pmhB (length=259) Species: 9606 (Homo sapiens) [Search protein sequence]
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTA
NVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDA
CEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWI
QKVIDQFGE
3D structure
PDB3pmh Binding of alpha-thrombin to surface-anchored platelet glycoprotein Ib(alpha) sulfotyrosines through a two-site mechanism involving exosite I.
ChainB
Resolution3.2 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 S195 G196
Catalytic site (residue number reindexed from 1) H43 D99 E202 G203 D204 S205 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 0G7 B H57 Y60A I174 D189 A190 E192 G193 S195 W215 G216 G219 H43 Y47 I179 D199 A200 E202 G203 S205 W227 G228 G230 BindingDB: IC50=1.5nM
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

View graph for
Biological Process
External links
PDB RCSB:3pmh, PDBe:3pmh, PDBj:3pmh
PDBsum3pmh
PubMed21555542
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

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