Structure of PDB 1smr Chain G

Receptor sequence
>1smrG (length=331) Species: 10090 (Mus musculus) [Search protein sequence]
TDLISPVVLTNYLNSQYYGEIGIGTPPQTFKVIFDTGSANLWVPSTKCSR
LYLACGIHSLYESSDSSSYMENGDDFTIHYGSGRVKGFLSQDSVTVGGIT
VTQTFGEVTQLPLIPFMLAQFDGVLGMGFPAQAVGGVTPVFDHILSQGVL
KEKVFSVYYNRGPHLLGGEVVLGGSDPQHYQGDFHYVSLSKTDSWQITMK
GVSVGSSTLLCEEGCEVVVDTGSSFISAPTSSLKLIMQALGAKEKRLHEY
VVSCSQVPTLPDISFNLGGRAYTLSSTDYVLQRDKLCTVALHAMDIPPPT
GPVWVLGATFIRKFYTEFDRHNNRIGFALAR
3D structure
PDB1smr X-ray analysis at 2.0 A resolution of mouse submaxillary renin complexed with a decapeptide inhibitor CH-66, based on the 4-16 fragment of rat angiotensinogen.
ChainG
Resolution2.0 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 S218
Catalytic site (residue number reindexed from 1) D35 S38 N40 W42 Y80 D220 S223
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 G S12 D32 G34 S35 I73 H74 Y75 G76 S77 P111 L114 A115 F117 Q128 D215 G217 S218 S219 F220 S222 P294 T295 V300 S15 D35 G37 S38 I78 H79 Y80 G81 S82 P115 L118 A119 F121 Q132 D220 G222 S223 S224 F225 S227 P299 T300 V305
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:1smr, PDBe:1smr, PDBj:1smr
PDBsum1smr
PubMed8107115
UniProtP00796|RENI2_MOUSE Renin-2 (Gene Name=Ren2)

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