Structure of PDB 3q7h Chain M

Receptor sequence
>3q7hM (length=192) Species: 360115 (Coxiella burnetii RSA 331) [Search protein sequence]
LVPMVVEQTSRGERAYDIYSRLLKDRVIFLVGQVEDHMANLAIAQMLFLE
SENPNKDINLYINSPGGAVTSAMAIYDTMQFVKPDVRTLCIGQAASAGAL
LLAGGAKGKRHCLPHSSVMIHQVLGGYQGQGTDIQIHAKQTQRVSDQLNQ
ILAKHTGKDIERVEKDTNRDYFLTPEEAVEYGLIDSIFKERP
3D structure
PDB3q7h Structure of the ClpP subunit of the ATP-dependent Clp Protease from Coxiella burnetii
ChainM
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 A100 H124 D173
Catalytic site (residue number reindexed from 1) G67 S96 A97 H121 D170
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 CA M M82 V85 K86 P87 M79 V82 K83 P84
BS02 CA M A71 V72 V126 L127 A68 V69 V123 L124
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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External links
PDB RCSB:3q7h, PDBe:3q7h, PDBj:3q7h
PDBsum3q7h
PubMed
UniProtQ83DJ2|CLPP_COXBU ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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