Structure of PDB 1sue Chain A

Receptor sequence
>1sueA (length=266) Species: 1390 (Bacillus amyloliquefaciens) [Search protein sequence]
AKCVSYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLNVAGGASF
VPSETNPFQDNNSHGTHVAGTVLAVAPSASLYAVKVLGADGSGQYSWIIN
GIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTS
GSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSICSTL
PGNKYGAKSGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENTTTKLGD
SFYYGKGLINVEAAAQ
3D structure
PDB1sue Mechanism of ionic strength dependence of crystal growth rates in a subtilisin variant.
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 N146 S212
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 DFP A H64 L126 N155 G219 S221 H64 L117 N146 G210 S212
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:1sue, PDBe:1sue, PDBj:1sue
PDBsum1sue
PubMed
UniProtP00782|SUBT_BACAM Subtilisin BPN' (Gene Name=apr)

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