BioLiP

Structure of PDB 2bkt Chain A

Receptor sequence

>2bktA (length=329) Species: 9606 (Homo sapiens) [Search protein sequence]

TSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYT
ACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQ
MFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKED
VFSFYYNRDSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVG
SSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNE
GPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGP
TWALGATFIRKFYTEFDRRNNRIGFALAR

3D structure

PDB

2bkt Equipotent Activity in Both Enantiomers of a Series of Ketopiperazine-Based Renin Inhibitors

Chain

Resolution

2.3 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 D219 A222
Catalytic site (residue number reindexed from 1)	D32 S35 N37 W39 Y77 D215 A218
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	RPF	A	Q14 D33 G35 W40 P42 H56 V106 M109 F114 A117 F119 D120 G121 V122 D219 G221	Q13 D32 G34 W39 P41 H55 V105 M108 F113 A116 F118 D119 G120 V121 D215 G217	MOAD: ic50=23nM PDBbind-CN: -logKd/Ki=7.64,IC50=23nM BindingDB: IC50=23nM

Gene Ontology

	Molecular Function
GO:0004190	aspartic-type endopeptidase activity

	Biological Process
GO:0006508	proteolysis

View graph for
Molecular Function

View graph for
Biological Process

PDB	RCSB:2bkt, PDBe:2bkt, PDBj:2bkt
PDBsum	2bkt
PubMed	15837327
UniProt	P00797\|RENI_HUMAN Renin (Gene Name=REN)