Structure of PDB 4rz1 Chain A

Receptor sequence
>4rz1A (length=336) Species: 9606 (Homo sapiens) [Search protein sequence]
TLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKC
SRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGG
ITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQG
VLKEDVFSFYYNRDSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQ
MKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFD
YVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMD
IPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR
3D structure
PDB4rz1 trans-3,4-Disubstituted pyrrolidines as inhibitors of the human aspartyl protease renin. Part II: Prime site exploration using an oxygen linker.
ChainA
Resolution2.6 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) D37 S40 N42 W44 Y82 D222 A225
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 3ZN A T12 Q13 V30 D32 G34 Y75 S76 T77 P111 L114 F117 L213 D215 G217 A218 I291 T17 Q18 V35 D37 G39 Y82 S83 T84 P117 L120 F123 L220 D222 G224 A225 I301 PDBbind-CN: -logKd/Ki=7.40,IC50=0.04uM
BindingDB: IC50=80nM
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:4rz1, PDBe:4rz1, PDBj:4rz1
PDBsum4rz1
PubMed25754490
UniProtP00797|RENI_HUMAN Renin (Gene Name=REN)

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