Structure of PDB 1be6 Chain A

Receptor sequence
>1be6A (length=274) Species: 1402 (Bacillus licheniformis) [Search protein sequence]
AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASF
VAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGS
GSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYARGVVVVA
AAGNSGNSGSTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAP
GAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLS
STATYLGSSFYYGKGLINVEAAAQ
3D structure
PDB1be6 Comparison of x-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water.
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 CCN A K136 D140 Y171 D172 K135 D139 Y170 D171
BS03 CCN A H64 S221 H63 S220
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1be6, PDBe:1be6, PDBj:1be6
PDBsum1be6
PubMed9789015
UniProtP00780|SUBC_BACLI Subtilisin Carlsberg (Gene Name=subC)

[Back to BioLiP]