Structure of PDB 1y34 Chain E

Receptor sequence
>1y34E (length=281) Species: 1390 (Bacillus amyloliquefaciens) [Search protein sequence]
AQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASM
VPSETNPFQDNNSHGTHVAGTVAALNNSIGVLGVAPSASLYAVKVLGADG
SGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVV
AAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMA
PGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPNWTNTQVRSSL
ENTTTKLGDSFYYGKGLINVQAAAQHHHHHH
3D structure
PDB1y34 Role of the intramolecular hydrogen bond network in the inhibitory power of chymotrypsin inhibitor 2
ChainE
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S221
Catalytic site (residue number reindexed from 1) S221
Enzyme Commision number 3.4.21.62: subtilisin.
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 CA E Q2 D41 L75 N77 I79 V81 Q2 D41 L75 N77 I79 V81
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1y34, PDBe:1y34, PDBj:1y34
PDBsum1y34
PubMed15865427
UniProtP00782|SUBT_BACAM Subtilisin BPN' (Gene Name=apr)

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