Structure of PDB 1gbb Chain A

Receptor sequence
>1gbbA (length=198) Species: 69 (Lysobacter enzymogenes) [Search protein sequence]
ANIVGGIEYSINNASLCSVGFSVTRGATKGFVTAGHCGTVNATARIGGAV
VGTFAARVFPGNDRAWVSLTSAQTLLPRVANGSSFVTVRGSTEAAVGAAV
CRSGRTTGYQCGTITAKNVTANYAEGAVRGLTQGNACAGRGDSGGSWITS
AGQAQGVMSGANVQSNGNNCGIPASQRSSLFERLQPILSQYGLSLVTG
3D structure
PDB1gbb Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 G193 S195 S214 G215 A216 H36 Y123 G141 S143 S159 G160 A161
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1gbb, PDBe:1gbb, PDBj:1gbb
PDBsum1gbb
PubMed7500345
UniProtP00778|PRLA_LYSEN Alpha-lytic protease (Gene Name=alpha-LP)

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