Structure of PDB 6iw7 Chain L

Receptor sequence
>6iw7L (length=193) Species: 83331 (Mycobacterium tuberculosis CDC1551) [Search protein sequence]
ILPSFIEHSSFGVKESNPYNKLFEERIIFLGVQVDDASANDIMAQLLVLE
SLDPDRDITMYINSPGGGFTSLMAIYDTMQYVRADIQTVCLGQAASAAAV
LLAAGTPGKRMALPNARVLIHQPSLSGVIQGQFSDLEIQAAEIERMRTLM
ETTLARHTGKDAGVIRKDTDRDKILTAEEAKDYGIIDTVLEYR
3D structure
PDB6iw7 structural insights into Mycobacterium tuberculosis ClpP1P2 inhibition by Cediranib: implications for developing antimicrobial agents targeting Clp protease
ChainL
Resolution2.69212 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 S0R L G81 P137 S138 M164 G67 P123 S124 M150
BS02 LEU L S138 L139 S124 L125
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:6iw7, PDBe:6iw7, PDBj:6iw7
PDBsum6iw7
PubMed
UniProtP9WPC3|CLPP2_MYCTU ATP-dependent Clp protease proteolytic subunit 2 (Gene Name=clpP2)

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