Structure of PDB 1au9 Chain A

Receptor sequence
>1au9A (length=275) Species: 1390 (Bacillus amyloliquefaciens) [Search protein sequence]
AQSVPYGVSQIKAPALHSQGYCGSNVKVAVIDSGIDSSHPDLKVAGGASF
VPSETNPFQDNNSHGTHVAGTVAALNNSIGVLGVAPCASLYAVKVLGADG
SGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVV
AAAGNEGTSGSSSTVGYPAKYPSVIAVGAVDSSNQRASFSSVGPELDVMA
PGVSICSTLPGNKYGAKSGTSMASPHVAGAAALILSKHPNWTNTQVRSSL
ENTTTKLGDSFYYGKGLINVQAAAQ
3D structure
PDB1au9 Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding.
ChainA
Resolution1.8 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 H64 N155 S221
Catalytic site (residue number reindexed from 1) D32 H64 N155 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 A Q2 D41 L75 N77 I79 V81 Q2 D41 L75 N77 I79 V81
BS02 CA A A169 Y171 V174 A176 D197 A169 Y171 V174 A176 D197
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:1au9, PDBe:1au9, PDBj:1au9
PDBsum1au9
PubMed2684274
UniProtP00782|SUBT_BACAM Subtilisin BPN' (Gene Name=apr)

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