Structure of PDB 6vgq Chain J

Receptor sequence
>6vgqJ (length=178) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
SLTDSVYERLLSERIIFLGSEVNDEIANRLCAQILLLAAEDASKDISLYI
NSPGGSISAGMAIYDTMVLAPCDIATYAMGMAASMGEFLLAAGTKGKRYA
LPHARILMHQPLGGVTGSAADIAIQAEQFAVIKKEMFRLNAEFTGQPIER
IEADSDRDRWFTAAEALEYGFVDHIITR
3D structure
PDB6vgq An allosteric switch regulatesMycobacterium tuberculosisClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR.
ChainJ
Resolution3.5 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) 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.
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 J G69 S70 I71 S98 H123 P125 L126 M150 G55 S56 I57 S84 H109 P111 L112 M136
BS02 peptide J S98 H123 S84 H109
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]