Structure of PDB 6nb1 Chain F

Receptor sequence
>6nb1F (length=183) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
LVPMVIFDIYSRLLKERVIFLTGQVEDHMANLIVAQMLFLEAENPEKDIY
LYINSPGGVITAGMSIYDTMQFIKPDVSTICMGQAASMGAFLLTAGAKGK
RFCLPNSRVMIHQPLGGYQGQATDIEIHAREILKVKGRMNELMALHTGQS
LEQIERDTERDRFLSAPEAVEYGLVDSILTHRN
3D structure
PDB6nb1 ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores.
ChainF
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G82 S111 M112 H136 D185
Catalytic site (residue number reindexed from 1) G58 S87 M88 H112 D161
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 KHS F R36 L37 E40 V42 Y74 Y76 F126 R206 R12 L13 E16 V18 Y50 Y52 F102 R182
BS02 KHS F F63 A66 F39 A42
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:0042802 identical protein binding
GO:0051117 ATPase binding
Biological Process
GO:0006508 proteolysis
GO:0006515 protein quality control for misfolded or incompletely synthesized proteins
GO:0009266 response to temperature stimulus
GO:0009314 response to radiation
GO:0009408 response to heat
GO:0010498 proteasomal protein catabolic process
GO:0043068 positive regulation of programmed cell death
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009368 endopeptidase Clp complex
GO:0009376 HslUV protease complex
GO:0016020 membrane

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Cellular Component
External links
PDB RCSB:6nb1, PDBe:6nb1, PDBj:6nb1
PDBsum6nb1
PubMed31925204
UniProtP0A6G7|CLPP_ECOLI ATP-dependent Clp protease proteolytic subunit (Gene Name=clpP)

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