Structure of PDB 4u0g Chain E Binding Site BS02

Receptor Information

>4u0g Chain E (length=197) Species: 83332 (Mycobacterium tuberculosis H37Rv)

ILPSFIEHSSFGVKESNPYNKLFEERIIFLGVQVDDASANDIMAQLLVLE
SLDPDRDITMYINSPGGGFTSLMAIYDTMQYVRADIQTVCLGQAASAAAV
LLAAGTPGKRMALPNARVLIHQPSLSGVIQGQFSDLEIQAAEIERMRTLM
ETTLARHTGKDAGVIRKDTDRDKILTAEEAKDYGIIDTVLEYRKLSA

Ligand information

>4u0g Chain g (length=6) Species: 32630 (synthetic construct)

FTPuAP

Receptor-Ligand Complex Structure

Structure summary

• 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): L61 Y95 R97
• Binding residue (residue number reindexed from 1): L47 Y81 R83

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

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)