Structure of PDB 6vgq Chain J Binding Site BS02

Receptor Information
>6vgq Chain J (length=178) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SLTDSVYERLLSERIIFLGSEVNDEIANRLCAQILLLAAEDASKDISLYI
NSPGGSISAGMAIYDTMVLAPCDIATYAMGMAASMGEFLLAAGTKGKRYA
LPHARILMHQPLGGVTGSAADIAIQAEQFAVIKKEMFRLNAEFTGQPIER
IEADSDRDRWFTAAEALEYGFVDHIITR
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]
PDB6vgq An allosteric switch regulatesMycobacterium tuberculosisClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR.
Resolution3.5 Å
Binding residue
(original residue number in PDB)
S98 H123
Binding residue
(residue number reindexed from 1)
S84 H109
Enzymatic activity
Catalytic site (original residue number in PDB) G69 S98 M99 H123 D172
Catalytic site (residue number reindexed from 1) G55 S84 M85 H109 D158
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:0005829 cytosol
GO:0005886 plasma membrane
GO:0009368 endopeptidase Clp complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6vgq, PDBe:6vgq, PDBj:6vgq
PDBsum6vgq
PubMed32123115
UniProtP9WPC5|CLPP1_MYCTU ATP-dependent Clp protease proteolytic subunit 1 (Gene Name=clpP1)

[Back to BioLiP]