Structure of PDB 4u0g Chain U Binding Site BS02

Receptor Information
>4u0g Chain U (length=196) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ILPSFIEHSSFGVKESNPYNKLFEERIIFLGVQVDDASANDIMAQLLVLE
SLDPDRDITMYINSPGGGFTSLMAIYDTMQYVRADIQTVCLGQAASAAAV
LLAAGTPGKRMALPNARVLIHQPSLSGVIQGQFSDLEIQAAEIERMRTLM
ETTLARHTGKDAGVIRKDTDRDKILTAEEAKDYGIIDTVLEYRKLS
Ligand information
Receptor-Ligand Complex Structure
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PDB4u0g Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery.
Resolution3.1978 Å
Binding residue
(original residue number in PDB)
L61 Y95 R97
Binding residue
(residue number reindexed from 1)
L47 Y81 R83
Enzymatic activity
Catalytic site (original residue number in PDB) G81 S110 A111 H135 D186
Catalytic site (residue number reindexed from 1) G67 S96 A97 H121 D172
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
PDBsum4u0g
PubMed25267638
UniProtP9WPC3|CLPP2_MYCTU ATP-dependent Clp protease proteolytic subunit 2 (Gene Name=clpP2)

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