Structure of PDB 4ryg Chain B

Receptor sequence
>4rygB (length=337) Species: 9606 (Homo sapiens) [Search protein sequence]
LTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSK
CSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVG
GITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQ
GVLKEDVFSFYYNRDSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQI
QMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLF
DYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAM
DIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR
3D structure
PDB4ryg trans-(3S,4S)-Disubstituted pyrrolidines as inhibitors of the human aspartyl protease renin. Part I: Prime site exploration using an amino linker.
ChainB
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) D38 S41 N43 W45 Y83 D223 A226
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 3ZJ B T12 Q13 Y14 V30 D32 G34 Y75 S76 T77 P111 L114 F117 L213 D215 G217 A218 I291 T295 T18 Q19 Y20 V36 D38 G40 Y83 S84 T85 P118 L121 F124 L221 D223 G225 A226 I302 T306 BindingDB: IC50=8.0nM
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:4ryg, PDBe:4ryg, PDBj:4ryg
PDBsum4ryg
PubMed25782742
UniProtP00797|RENI_HUMAN Renin (Gene Name=REN)

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