Structure of PDB 2pgq Chain B

Receptor sequence
>2pgqB (length=257) Species: 9606 (Homo sapiens) [Search protein sequence]
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTA
NVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDA
AEGDSGGPFVMKSPFNNRWYQMGIVSWGEGADRDGKYGFYTHVFRLKKWI
QKVIDQF
3D structure
PDB2pgq Important role of the cys-191 cys-220 disulfide bond in thrombin function and allostery
ChainB
Resolution1.8 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 0G6 B H57 Y60A W60D N98 L99 D189 A190 E192 S195 S214 W215 G216 H43 Y47 W50 N95 L96 D199 A200 E202 S205 S226 W227 G228
BS02 ZN B H71 E77 H66 E72
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:2pgq, PDBe:2pgq, PDBj:2pgq
PDBsum2pgq
PubMed17636263
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

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