Structure of PDB 4u0g Chain R Binding Site BS01
Receptor Information
>4u0g Chain R (length=196) Species:
83332
(Mycobacterium tuberculosis H37Rv) [
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ILPSFIEHSSFGVKESNPYNKLFEERIIFLGVQVDDASANDIMAQLLVLE
SLDPDRDITMYINSPGGGFTSLMAIYDTMQYVRADIQTVCLGQAASAAAV
LLAAGTPGKRMALPNARVLIHQPSLSGVIQGQFSDLEIQAAEIERMRTLM
ETTLARHTGKDAGVIRKDTDRDKILTAEEAKDYGIIDTVLEYRKLS
Ligand information
>4u0g Chain l (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)
E39 I41 Y75 Q101 L105 M125 R207
Binding residue
(residue number reindexed from 1)
E25 I27 Y61 Q87 L91 M111 R193
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
PDBsum
4u0g
PubMed
25267638
UniProt
P9WPC3
|CLPP2_MYCTU ATP-dependent Clp protease proteolytic subunit 2 (Gene Name=clpP2)
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