Structure of PDB 1ny2 Chain 2

Receptor sequence
>1ny22 (length=259) Species: 9606 (Homo sapiens) [Search protein sequence]
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTA
NVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDA
CEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWI
QKVIDQFGE
3D structure
PDB1ny2 Mechanisms of Arg-Pro-Pro-Gly-Phe inhibition of thrombin.
Chain2
Resolution2.3 Å
3D
structure
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Enzymatic activity
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 2 F34 K36 L65 R67 R73 T74 Y76 I82 F19 K21 L60 R62 R68 T69 Y71 I78
BS02 peptide 2 H57 W60D D189 A190 C191 E192 S195 S214 W215 G216 H43 W50 D199 A200 C201 E202 S205 S226 W227 G228
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:1ny2, PDBe:1ny2, PDBj:1ny2
PDBsum1ny2
PubMed12598231
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

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