Structure of PDB 1bil Chain A

Receptor sequence
>1bilA (length=334) Species: 9606 (Homo sapiens) [Search protein sequence]
GNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSR
LYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGIT
VTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVL
KEDVFSFYYNRDSESLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMK
GVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYV
VKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIP
PPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR
3D structure
PDB1bil Crystallographic studies on the binding modes of P2-P3 butanediamide renin inhibitors.
ChainA
Resolution2.4 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) D35 S38 N40 W42 Y80 D220 A223
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 0IU A D32 Y75 S76 T77 P111 F117 D215 G217 A218 S219 Y220 S222 M289 A300 D35 Y80 S81 T82 P115 F121 D220 G222 A223 S224 Y225 S227 M297 A308 MOAD: ic50=0.5nM
PDBbind-CN: -logKd/Ki=9.30,IC50=0.5nM
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:1bil, PDBe:1bil, PDBj:1bil
PDBsum1bil
PubMed7493993
UniProtP00797|RENI_HUMAN Renin (Gene Name=REN)

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