Structure of PDB 3p2l Chain F

Receptor sequence
>3p2lF (length=183) Species: 177416 (Francisella tularensis subsp. tularensis SCHU S4) [Search protein sequence]
VPTVIFDIYSRLLKERIVFLNGEVNDHSANLVIAQLLFLESEDPDKDIYF
YINSPGGMVTAGMGVYDTMQFIKPDVSTICIGLAASMGSLLLAGGAKGKR
YSLPSSQIMIHQPLGGFRGQASDIEIHAKNILRIKDRLNKVLAHHTGQDL
ETIVKDTDRDNFMMADEAKAYGLIDHVIESREA
3D structure
PDB3p2l Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis
ChainF
Resolution2.295 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G72 S101 M102 H126 D175
Catalytic site (residue number reindexed from 1) G57 S86 M87 H111 D160
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 MG F M84 I87 P89 M69 I72 P74
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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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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