Structure of PDB 2zl2 Chain N

Receptor sequence
>2zl2N (length=173) Species: 210 (Helicobacter pylori) [Search protein sequence]
DIYSRLLKDRIVLLSGEINDSVASSIVAQLLFLEAEDPEKDIGLYINSPG
GVITSGLSIYDTMNFIRPDVSTICIGQAASMGAFLLSCGAKGKRFSLPHS
RIMIHQPLGGAQGQASDIEIISNEILRLKGLMNSILAQNSGQSLEQIAKD
TDRDFYMSAKEAKEYGLIDKVLQ
3D structure
PDB2zl2 The structural basis for the activation and peptide recognition of bacterial ClpP
ChainN
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G70 S99 M100 H124 D173
Catalytic site (residue number reindexed from 1) G51 S80 M81 H105 D154
Enzyme Commision number 3.4.21.92: endopeptidase Clp.
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 N G70 V71 I72 S99 M100 H124 P126 L127 G51 V52 I53 S80 M81 H105 P107 L108
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

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Cellular Component
External links
PDB RCSB:2zl2, PDBe:2zl2, PDBj:2zl2
PDBsum2zl2
PubMed18468623
UniProtP56156|CLPP_HELPY ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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