Structure of PDB 1gbb Chain A Binding Site BS01

Receptor Information
>1gbb Chain A (length=198) Species: 69 (Lysobacter enzymogenes) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ANIVGGIEYSINNASLCSVGFSVTRGATKGFVTAGHCGTVNATARIGGAV
VGTFAARVFPGNDRAWVSLTSAQTLLPRVANGSSFVTVRGSTEAAVGAAV
CRSGRTTGYQCGTITAKNVTANYAEGAVRGLTQGNACAGRGDSGGSWITS
AGQAQGVMSGANVQSNGNNCGIPASQRSSLFERLQPILSQYGLSLVTG
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1gbb Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
Resolution2.15 Å
Binding residue
(original residue number in PDB)
H57 Y171 G193 S195 S214 G215 A216
Binding residue
(residue number reindexed from 1)
H36 Y123 G141 S143 S159 G160 A161
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.
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:1gbb, PDBe:1gbb, PDBj:1gbb
PDBsum1gbb
PubMed7500345
UniProtP00778|PRLA_LYSEN Alpha-lytic protease (Gene Name=alpha-LP)

[Back to BioLiP]