Structure of PDB 1sua Chain A

Receptor sequence
>1suaA (length=263) Species: 1390 (Bacillus amyloliquefaciens) [Search protein sequence]
VPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLNVAGGASFVPS
ETNPFQDNNSHGTHVAGTVLAVAPSASLYAVKVLGADGSGQYSWIINGIE
WAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSS
STVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSIVSTLPGN
KYGAKSGTAMASPHVAGAAALILSKHPNWTNTQVRSSLENTTTKLGDSFY
YGKGLINVEAAAQ
3D structure
PDB1sua Crystal structure of calcium-independent subtilisin BPN' with restored thermal stability folded without the prodomain.
ChainA
Resolution2.1 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 A221
Catalytic site (residue number reindexed from 1) D29 H61 N143 A209
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 peptide A H64 G100 S101 G102 Y104 S125 L126 G127 G154 N155 A221 H61 G88 S89 G90 Y92 S113 L114 G115 G142 N143 A209
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:1sua, PDBe:1sua, PDBj:1sua
PDBsum1sua
PubMed9552156
UniProtP00782|SUBT_BACAM Subtilisin BPN' (Gene Name=apr)

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