Structure of PDB 2zl4 Chain I Binding Site BS01

Receptor Information
>2zl4 Chain I (length=173) Species: 210 (Helicobacter pylori) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DIYSRLLKDRIVLLSGEINDSVASSIVAQLLFLEAEDPEKDIGLYINSPG
GVITSGLSIYDTMNFIRPDVSTICIGQAAAMGAFLLSCGAKGKRFSLPHS
RIMIHQPLGGAQGQASDIEIISNEILRLKGLMNSILAQNSGQSLEQIAKD
TDRDFYMSAKEAKEYGLIDKVLQ
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]
PDB2zl4 The structural basis for the activation and peptide recognition of bacterial ClpP
Resolution2.5 Å
Binding residue
(original residue number in PDB)		G70 I72 A99 M100 H124 P126 L127
Binding residue
(residue number reindexed from 1)		G51 I53 A80 M81 H105 P107 L108
Enzymatic activity
Catalytic site (original residue number in PDB) G70 A99 M100 H124 D173
Catalytic site (residue number reindexed from 1) G51 A80 M81 H105 D154
Enzyme Commision number 3.4.21.92: endopeptidase Clp.
Gene Ontology
Molecular Function
GO:0004176 ATP-dependent peptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0051117 ATPase binding
Biological Process
GO:0006508 proteolysis
GO:0006515 protein quality control for misfolded or incompletely synthesized proteins
Cellular Component
GO:0005737 cytoplasm
GO:0009368 endopeptidase Clp complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2zl4, PDBe:2zl4, PDBj:2zl4
PDBsum2zl4
PubMed18468623
UniProtP56156|CLPP_HELPY ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

[Back to BioLiP]