Structure of PDB 1scn Chain E

Receptor sequence
>1scnE (length=274) Species: 1402 (Bacillus licheniformis) [Search protein sequence]
AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASF
VAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGS
GSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYARGVVVVA
AAGNSGNSGSTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAP
GAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLS
STATYLGSSFYYGKGLINVEAAAQ
3D structure
PDB1scn Inactivation of subtilisin Carlsberg by N-((tert-butoxycarbonyl)alanylprolylphenylalanyl)-O-benzolhydroxyl- amine: formation of a covalent enzyme-inhibitor linkage in the form of a carbamate derivative.
ChainE
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S221
Catalytic site (residue number reindexed from 1) 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 0EF E G100 L126 G127 A152 G154 N155 S221 G99 L125 G126 A151 G153 N154 S220
BS02 CA E Q2 D41 L75 N77 T79 V81 Q2 D41 L74 N76 T78 V80
BS03 CA E A37 S38 H39 L42 A37 S38 H39 L42
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:1scn, PDBe:1scn, PDBj:1scn
PDBsum1scn
PubMed8068694
UniProtP00780|SUBC_BACLI Subtilisin Carlsberg (Gene Name=subC)

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