Structure of PDB 3q7h Chain K

Receptor sequence
>3q7hK (length=189) Species: 360115 (Coxiella burnetii RSA 331) [Search protein sequence]
VLVPMVVEQTRAYDIYSRLLKDRVIFLVGQVEDHMANLAIAQMLFLESEN
PNKDINLYINSPGGAVTSAMAIYDTMQFVKPDVRTLCIGQAASAGALLLA
GGAKGKRHCLPHSSVMIHQVLGGYQGQGTDIQIHAKQTQRVSDQLNQILA
KHTGKDIERVEKDTNRDYFLTPEEAVEYGLIDSIFKERP
3D structure
PDB3q7h Structure of the ClpP subunit of the ATP-dependent Clp Protease from Coxiella burnetii
ChainK
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) G70 S99 A100 H124 D173
Catalytic site (residue number reindexed from 1) G64 S93 A94 H118 D167
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 K M82 V85 P87 M76 V79 P81
BS02 CA K A71 V72 V126 L127 A65 V66 V120 L121
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:3q7h, PDBe:3q7h, PDBj:3q7h
PDBsum3q7h
PubMed
UniProtQ83DJ2|CLPP_COXBU ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

[Back to BioLiP]