Structure of PDB 1ook Chain B Binding Site BS01
Receptor Information
>1ook Chain B (length=259) Species:
9606
(Homo sapiens) [
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IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTA
NVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDA
CEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWI
QKVIDQFGE
Ligand information
>1ook Chain P (length=3) [
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FPR
Receptor-Ligand Complex Structure
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PDB
1ook
Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
H57 Y60A L99 I174 D189 A190 S195 W215 G216
Binding residue
(residue number reindexed from 1)
H43 Y47 L96 I179 D199 A200 S205 W227 G228
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.
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:1ook
,
PDBe:1ook
,
PDBj:1ook
PDBsum
1ook
PubMed
12855810
UniProt
P00734
|THRB_HUMAN Prothrombin (Gene Name=F2)
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