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Structure of PDB 8et3 Chain A Binding Site BS01

Receptor Information
>8et3 Chain A (length=343) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LPTPHEIRNHLDDYVIGQEQAKKVLAVAVYNHYKRLRNLGKSNILLIGPT
GSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVENIIQKLLQKCDY
DVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAA
VPPQGGRKHPQQEFLQVDTSKILFICGGAFAGLDKVISHRVETGSGIGFG
ATVKAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVVATLNELSEEA
LIQILKEPKNALTKQYQALFNLEGVDLEFRDEALDAIAKKAMARKTGARG
LRSIVEAALLDTMYDLPSMEDVEKVVIDESVIDGQSEPLLIYG
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB8et3 The SspB adaptor drives structural changes in the AAA+ ClpXP protease during ssrA-tagged substrate delivery.
Resolution3.7 Å
Binding residue
(original residue number in PDB)
G152 Y153 V154 I198 T199
Binding residue
(residue number reindexed from 1)
G81 Y82 V83 I127 T128
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0002020 protease binding
GO:0004176 ATP-dependent peptidase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016887 ATP hydrolysis activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0046983 protein dimerization activity
GO:0051082 unfolded protein binding
GO:0097718 disordered domain specific binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0030164 protein denaturation
GO:0043335 protein unfolding
GO:0051301 cell division
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0005829 cytosol
GO:0009368 endopeptidase Clp complex
GO:0009376 HslUV protease complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:8et3, PDBe:8et3, PDBj:8et3
PDBsum8et3
PubMed36730206
UniProtP0A6H1|CLPX_ECOLI ATP-dependent Clp protease ATP-binding subunit ClpX (Gene Name=clpX)

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