Structure of PDB 2il2 Chain A

Receptor sequence
>2il2A (length=338) Species: 9606 (Homo sapiens) [Search protein sequence]
LGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCS
RLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGI
TVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGV
LKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQ
IQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRL
FDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHA
MDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR
3D structure
PDB2il2 Binding thermodynamics of substituted diaminopyrimidine renin inhibitors.
ChainA
Resolution2.24 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D33 S36 N38 W40 Y78 D221 A224
Catalytic site (residue number reindexed from 1) D36 S39 N41 W43 Y81 D224 A227
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 LIX A T13 Q14 Y15 V31 D33 G35 Y78 S79 T80 L116 F119 V122 D221 G223 S225 F248 H296 T16 Q17 Y18 V34 D36 G38 Y81 S82 T83 L119 F122 V125 D224 G226 S228 F251 H299 MOAD: Kd=79nM
BindingDB: IC50=27nM,Kd=79nM
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:2il2, PDBe:2il2, PDBj:2il2
PDBsum2il2
PubMed17113558
UniProtP00797|RENI_HUMAN Renin (Gene Name=REN)

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