Structure of PDB 3vcm Chain B

Receptor sequence
>3vcmB (length=325) Species: 9606 (Homo sapiens) [Search protein sequence]
VILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACV
YHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFG
EVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFS
FYYNRDSGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTL
LCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTL
PDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWAL
GATFIRKFYTEFDRRNNRIGFALAR
3D structure
PDB3vcm Human Prorenin Structure Sheds Light on a Novel Mechanism of Its Autoinhibition and on Its Non-Proteolytic Activation by the (Pro)renin Receptor.
ChainB
Resolution2.93 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) D29 S32 N34 W36 Y74 D211 A214
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 peptide B M10 D11 T12 Q13 Y14 Y15 E17 F31 G92 I94 L110 L114 A115 E116 S159 G163 Q164 I165 V166 L167 D171 F243 H287 M7 D8 T9 Q10 Y11 Y12 E14 F28 G91 I93 L108 L112 A113 E114 S157 G159 Q160 I161 V162 L163 D167 F238 H286
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:3vcm, PDBe:3vcm, PDBj:3vcm
PDBsum3vcm
PubMed22575890
UniProtP00797|RENI_HUMAN Renin (Gene Name=REN)

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