Structure of PDB 4u0g Chain Z

Receptor sequence
>4u0gZ (length=175) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
TDSVYERLLSERIIFLGSEVNDEIANRLCAQILLLAAEDASKDISLYINS
PGGSISAGMAIYDTMVLAPCDIATYAMGMAASMGEFLLAAGTKGKRYALP
HARILMHQPLGGVTGSAADIAIQAEQFAVIKKEMFRLNAEFTGQPIERIE
ADSDRDRWFTAAEALEYGFVDHIIT
3D structure
PDB4u0g Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery.
ChainZ
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) G69 S98 M99 H123 D172
Catalytic site (residue number reindexed from 1) G53 S82 M83 H107 D156
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 ZIL Z G69 S70 I71 M99 H123 L126 I146 G53 S54 I55 M83 H107 L110 I130
Gene Ontology
Molecular Function
GO:0004176 ATP-dependent peptidase activity
GO:0004252 serine-type endopeptidase activity
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: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
UniProtP9WPC5|CLPP1_MYCTU ATP-dependent Clp protease proteolytic subunit 1 (Gene Name=clpP1)

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