BioLiP

Structure of PDB 1gbc Chain A Binding Site BS01

Receptor Information

>1gbc 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

>1gbc Chain P (length=4) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

AAPL

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1gbc Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
Resolution	2.2 Å
Binding residue (original residue number in PDB)	H57 Y171 G191 G193 S195 S214 G215 A216
Binding residue (residue number reindexed from 1)	H36 Y123 G139 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

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Molecular Function

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Biological Process

PDB	RCSB:1gbc, PDBe:1gbc, PDBj:1gbc
PDBsum	1gbc
PubMed	7500345
UniProt	P00778\|PRLA_LYSEN Alpha-lytic protease (Gene Name=alpha-LP)