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

PDB

1ny2 Mechanisms of Arg-Pro-Pro-Gly-Phe inhibition of thrombin.

Chain

Resolution

2.3 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
PDBsum	1ny2
PubMed	12598231
UniProt	P00734\|THRB_HUMAN Prothrombin (Gene Name=F2)

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