Structure of PDB 3p2l Chain B

Receptor sequence
>3p2lB (length=184) Species: 177416 (Francisella tularensis subsp. tularensis SCHU S4) [Search protein sequence]
LVPTVIAFDIYSRLLKERIVFLNGEVNDHSANLVIAQLLFLESEDPDKDI
YFYINSPGGMVTAGMGVYDTMQFIKPDVSTICIGLAASMGSLLLAGGAKG
KRYSLPSSQIMIHQPLGGFRGQASDIEIHAKNILRIKDRLNKVLAHHTGQ
DLETIVKDTDRDNFMMADEAKAYGLIDHVIESRE
3D structure
PDB3p2l Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis
ChainB
Resolution2.295 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
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 B M84 I87 P89 M71 I74 P76
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
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)

[Back to BioLiP]