Structure of PDB 3lpr Chain A

Receptor sequence
>3lprA (length=198) Species: 69 (Lysobacter enzymogenes) [Search protein sequence]
ANIVGGIEYSINNASLCSVGFSVTRGATKGFVTAGHCGTVNATARIGGAV
VGTFAARVFPGNDRAWVSLTSAQTLLPRVANGSSFVTVRGSTEAAVGAAV
CRSGRTTGYQCGTITAKNVTANYAEGAVRGLTQGNACAGRGDSGGSWITS
AGQAQGVMSGGNVQSNGNNCGIPASQRSSLFERLQPILSQYGLSLVTG
3D structure
PDB3lpr Structural basis for broad specificity in alpha-lytic protease mutants.
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) H57 D102 G193 S195 S214
Catalytic site (residue number reindexed from 1) H36 D63 G141 S143 S159
Enzyme Commision number 3.4.21.12: alpha-lytic endopeptidase.
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 H57 Y171 G192A G193 S195 S214 G215 G216 V217A H36 Y123 G139 G141 S143 S159 G160 G161 V163
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3lpr, PDBe:3lpr, PDBj:3lpr
PDBsum3lpr
PubMed1931963
UniProtP00778|PRLA_LYSEN Alpha-lytic protease (Gene Name=alpha-LP)

[Back to BioLiP]