Structure of PDB 1bh6 Chain A

Receptor sequence
>1bh6A (length=274) Species: 1402 (Bacillus licheniformis) [Search protein sequence]
AQTVPYGIPLIKADKVQAQGYKGANVKVGIIDTGIASSHTDLKVVGGASF
VSGESYNTDGNGHGTHVAGTVAALDNTTGVLGVAPNVSLYAIKVLNSSGS
GSYSAIVSGIEWATQNGLDVINMSLGGPSGSTALKQAVDKAYASGIVVVA
AAGNSGNSGSQNTIGYPAKYDSVIAVGAVDSNKNRASFSSVGSELEVMAP
GVSVYSTYPSNTYTSLNGTSMASPHVAGAAALILSKYPTLSASQVRNRLS
STATNLGDSFYYGKGLINVEAAAQ
3D structure
PDB1bh6 Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg.
ChainA
Resolution1.75 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 H63 N154 S220
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 T79 V81 Q2 D41 L74 N76 T78 V80
BS02 1BH A H64 G100 Y104 I107 S125 L126 G127 G128 A152 G154 N155 S221 H63 G99 Y103 I106 S124 L125 G126 G127 A151 G153 N154 S220
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0030435 sporulation resulting in formation of a cellular spore
Cellular Component
GO:0005576 extracellular region

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1bh6, PDBe:1bh6, PDBj:1bh6
PDBsum1bh6
PubMed9826175
UniProtP00781|SUBD_BACLI Subtilisin DY (Gene Name=apr)

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