Structure of PDB 4u0g Chain B

Receptor sequence
>4u0gB (length=197) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
YILPSFIEHSSFGVKESNPYNKLFEERIIFLGVQVDDASANDIMAQLLVL
ESLDPDRDITMYINSPGGGFTSLMAIYDTMQYVRADIQTVCLGQAASAAA
VLLAAGTPGKRMALPNARVLIHQPSLSGVIQGQFSDLEIQAAEIERMRTL
METTLARHTGKDAGVIRKDTDRDKILTAEEAKDYGIIDTVLEYRKLS
3D structure
PDB4u0g Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery.
ChainB
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) G68 S97 A98 H122 D173
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 B E39 Y75 Q101 L105 L204 R207 E26 Y62 Q88 L92 L191 R194
BS02 peptide B L61 Y95 R97 L48 Y82 R84
BS03 ZIL B G81 G82 T84 P137 S138 I157 M160 G68 G69 T71 P124 S125 I144 M147
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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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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