Structure of PDB 4u0g Chain B Binding Site BS02
Receptor Information
>4u0g Chain B (length=197) Species:
83332
(Mycobacterium tuberculosis H37Rv) [
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YILPSFIEHSSFGVKESNPYNKLFEERIIFLGVQVDDASANDIMAQLLVL
ESLDPDRDITMYINSPGGGFTSLMAIYDTMQYVRADIQTVCLGQAASAAA
VLLAAGTPGKRMALPNARVLIHQPSLSGVIQGQFSDLEIQAAEIERMRTL
METTLARHTGKDAGVIRKDTDRDKILTAEEAKDYGIIDTVLEYRKLS
Ligand information
>4u0g Chain d (length=6) Species:
32630
(synthetic construct) [
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FTPuAP
Receptor-Ligand Complex Structure
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PDB
4u0g
Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery.
Resolution
3.1978 Å
Binding residue
(original residue number in PDB)
L61 Y95 R97
Binding residue
(residue number reindexed from 1)
L48 Y82 R84
Enzymatic activity
Catalytic site (original residue number in PDB)
G81 S110 A111 H135 D186
Catalytic site (residue number reindexed from 1)
G68 S97 A98 H122 D173
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:4u0g
,
PDBe:4u0g
,
PDBj:4u0g
PDBsum
4u0g
PubMed
25267638
UniProt
P9WPC3
|CLPP2_MYCTU ATP-dependent Clp protease proteolytic subunit 2 (Gene Name=clpP2)
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