Structure of PDB 3st9 Chain B

Receptor sequence
>3st9B (length=170) Species: 196620 (Staphylococcus aureus subsp. aureus MW2) [Search protein sequence]
YDIYSRLLKDRIIMLGSQIDDNVANSIVSQLLFLQAQDSEKDIYLYINSP
GGSVTAGFAIYDTIQHIKPDVQTICIGMAASMGSFLLAAGAKGKRFALPN
AEVMIHQPGQATEIEIAANHILKTREKLNRILSERTGQSIEKIQKDTDRD
NFLTAEEAKEYGLIDEVMVP
3D structure
PDB3st9 Structural switching of Staphylococcus aureus Clp protease: a key to understanding protease dynamics
ChainB
Resolution2.43 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G69 S98 M99 H123 D172
Catalytic site (residue number reindexed from 1) G52 S81 M82 H106 D150
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 CA B K58 D59 K41 D42
Gene Ontology
Molecular Function
GO:0004176 ATP-dependent peptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0042802 identical protein binding
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:3st9, PDBe:3st9, PDBj:3st9
PDBsum3st9
PubMed21900233
UniProtP63786|CLPP_STAAW ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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