Structure of PDB 8et3 Chain B Binding Site BS01

Receptor Information

>8et3 Chain B (length=352) Species: 562 (Escherichia coli)

ALPTPHEIRNHLDDYVIGQEQAKKVLAVAVYNHYKRLRNGDTSNGVELGK
SNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVENII
QKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALL
KLIEGTVAAVPPQGGRKHPQQEFLQVDTSKILFICGGAFAGLDKVISHRV
ETGSGIGFGATVKAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVVA
TLNELSEEALIQILKEPKNALTKQYQALFNLEGVDLEFRDEALDAIAKKA
MARKTGARGLRSIVEAALLDTMYDLPSMEDVEKVVIDESVIDGQSEPLLI
YG

Ligand information

>8et3 Chain S (length=11) Species: 562 (Escherichia coli)

AANDENYALAA

Receptor-Ligand Complex Structure

Structure summary

• PDB: 8et3 The SspB adaptor drives structural changes in the AAA+ ClpXP protease during ssrA-tagged substrate delivery.
• Resolution: 3.7 Å
• Binding residue (original residue number in PDB): Y153 V154
• Binding residue (residue number reindexed from 1): Y91 V92

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

External links

• PDB: RCSB:8et3, PDBe:8et3, PDBj:8et3
• PDBsum: 8et3
• PubMed: 36730206
• UniProt: P0A6H1|CLPX_ECOLI ATP-dependent Clp protease ATP-binding subunit ClpX (Gene Name=clpX)