Structure of PDB 4u0g Chain Q

Receptor sequence
>4u0gQ (length=195) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
ILPSFIEHSSFGVKESNPYNKLFEERIIFLGVQVDDASANDIMAQLLVLE
SLDPDRDITMYINSPGGGFTSLMAIYDTMQYVRADIQTVCLGQAASAAAV
LLAAGTPGKRMALPNARVLIHQPSLSGVIQGQFSDLEIQAAEIERMRTLM
ETTLARHTGKDAGVIRKDTDRDKILTAEEAKDYGIIDTVLEYRKL
3D structure
PDB4u0g Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery.
ChainQ
Resolution3.1978 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 Q E39 Y75 Q101 L105 M125 E25 Y61 Q87 L91 M111
BS02 peptide Q L61 Y95 R97 L47 Y81 R83
BS03 ZIL Q G81 G82 F83 T84 P137 S138 I157 M160 M164 G67 G68 F69 T70 P123 S124 I143 M146 M150
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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