Structure of PDB 3p2l Chain B Binding Site BS01

Receptor Information
>3p2l Chain B (length=184) Species: 177416 (Francisella tularensis subsp. tularensis SCHU S4) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LVPTVIAFDIYSRLLKERIVFLNGEVNDHSANLVIAQLLFLESEDPDKDI
YFYINSPGGMVTAGMGVYDTMQFIKPDVSTICIGLAASMGSLLLAGGAKG
KRYSLPSSQIMIHQPLGGFRGQASDIEIHAKNILRIKDRLNKVLAHHTGQ
DLETIVKDTDRDNFMMADEAKAYGLIDHVIESRE
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain3p2l Chain B Residue 202 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3p2l Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis
Resolution2.295 Å
Binding residue
(original residue number in PDB)		M84 I87 P89
Binding residue
(residue number reindexed from 1)		M71 I74 P76
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) G72 S101 M102 H126 D175
Catalytic site (residue number reindexed from 1) G59 S88 M89 H113 D162
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: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:0009368 endopeptidase Clp complex

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Cellular Component
External links
PDB RCSB:3p2l, PDBe:3p2l, PDBj:3p2l
PDBsum3p2l
PubMed
UniProtQ5NH47|CLPP_FRATT ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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