Structure of PDB 1gbi Chain A Binding Site BS01
Receptor Information
>1gbi Chain A (length=198) Species:
69
(Lysobacter enzymogenes) [
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ANIVGGIEYSINNASLCSVGFSVTRGATKGFVTAGHCGTVNATARIGGAV
VGTFAARVFPGNDRAWVSLTSAQTLLPRVANGSSFVTVRGSTEAAVGAAV
CRSGRTTGYQCGTITAKNVTANYAEGAVRGLTQGNACAGRGDSGGSWITS
AGQAQGVMSGLNVQSNGNNCGIPASQRSSLFERLQPILSQYGLSLVTG
Ligand information
>1gbi Chain P (length=4) [
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AAPF
Receptor-Ligand Complex Structure
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PDB
1gbi
Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
H57 Y171 R192 S195 S214 G215 L216 V218
Binding residue
(residue number reindexed from 1)
H36 Y123 R140 S143 S159 G160 L161 V163
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
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Molecular Function
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Biological Process
External links
PDB
RCSB:1gbi
,
PDBe:1gbi
,
PDBj:1gbi
PDBsum
1gbi
PubMed
7500345
UniProt
P00778
|PRLA_LYSEN Alpha-lytic protease (Gene Name=alpha-LP)
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