Structure of PDB 6vgn Chain F Binding Site BS01
Receptor Information
>6vgn Chain F (length=196) Species:
1773
(Mycobacterium tuberculosis) [
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ILPSFIEHSSFGVKESNPYNKLFEERIIFLGVQVDDASANDIMAQLLVLE
SLDPDRDITMYINSPGGGFTSLMAIYDTMQYVRADIQTVCLGQAASAAAV
LLAAGTPGKRMALPNARVLIHQPSLSGVIQGQFSDLEIQAAEIERMRTLM
ETTLARHTGKDAGVIRKDTDRDKILTAEEAKDYGIIDTVLEYRKLS
Ligand information
>6vgn Chain X (length=7) Species:
32630
(synthetic construct) [
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tFTPKAK
Receptor-Ligand Complex Structure
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PDB
6vgn
An allosteric switch regulatesMycobacterium tuberculosisClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR.
Resolution
3.1 Å
Binding residue
(original residue number in PDB)
S65 Y95
Binding residue
(residue number reindexed from 1)
S51 Y81
Enzymatic activity
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:0005515
protein binding
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:0009274
peptidoglycan-based cell wall
GO:0009368
endopeptidase Clp complex
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6vgn
,
PDBe:6vgn
,
PDBj:6vgn
PDBsum
6vgn
PubMed
32123115
UniProt
P9WPC3
|CLPP2_MYCTU ATP-dependent Clp protease proteolytic subunit 2 (Gene Name=clpP2)
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