Structure of PDB 1c3l Chain A

Receptor sequence
>1c3lA (length=274) Species: 1402 (Bacillus licheniformis) [Search protein sequence]
AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASF
VAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGS
GSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYARGVVVVA
AAGNSGSSGSTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAP
GAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLS
STATYLGSSFYYGKGLINVEAAAQ
3D structure
PDB1c3l Exploring hydrophobic sites in proteins with xenon or krypton.
ChainA
Resolution2.16 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 CA A A169 K170 Y171 D172 V174 A168 K169 Y170 D171 V173
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:1c3l, PDBe:1c3l, PDBj:1c3l
PDBsum1c3l
PubMed9443341
UniProtP00780|SUBC_BACLI Subtilisin Carlsberg (Gene Name=subC)

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