Structure of PDB 4pyv Chain A

Receptor sequence
>4pyvA (length=335) Species: 9606 (Homo sapiens) [Search protein sequence]
LGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCS
RLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGI
TVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGV
LKEDVFSFYYNRDSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQM
KGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDY
VVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDI
PPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR
3D structure
PDB4pyv Structure-based design of substituted piperidines as a new class of highly efficacious oral direct Renin inhibitors.
ChainA
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D32 S35 N37 W39 Y75 D215 A218
Catalytic site (residue number reindexed from 1) D36 S39 N41 W43 Y81 D221 A224
Enzyme Commision number 3.4.23.15: renin.
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 2XF A V30 D32 G34 R74 Y75 T77 P111 F117 D215 G217 V34 D36 G38 R80 Y81 T83 P116 F122 D221 G223 PDBbind-CN: -logKd/Ki=6.70,IC50=200nM
BindingDB: IC50=200nM
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:4pyv, PDBe:4pyv, PDBj:4pyv
PDBsum4pyv
PubMed25050166
UniProtP00797|RENI_HUMAN Renin (Gene Name=REN)

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