29HB image
Deposition Date 2026-03-11
Release Date 2026-04-22
Last Version Date 2026-04-22
Entry Detail
PDB ID:
29HB
Keywords:
Title:
Cryo-EM structure of the ClpE/ClpP degradation complex from E.faecalis
Biological Source:
Source Organism(s):
Enterobacter (Taxon ID: 547)
Expression System(s):
Method Details:
Experimental Method:
Resolution:
2.80 Å
Aggregation State:
PARTICLE
Reconstruction Method:
SINGLE PARTICLE
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:ATP-dependent Clp protease pr
Gene (Uniprot):clpP
Chain IDs:A, B, C, D, E, F, G, I, J (auth: K), K (auth: L), L (auth: M), M (auth: N), N (auth: S), O (auth: T)
Chain Length:197
Number of Molecules:14
Biological Source:Enterobacter
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:unknown substrate bound to Cl
Chain IDs:H
Chain Length:16
Number of Molecules:1
Biological Source:Enterobacter
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:ATP-dependent Clp protease, A
Gene (Uniprot):clpE
Chain IDs:P (auth: b), Q (auth: c), R (auth: d), S (auth: a), T (auth: e), U (auth: f)
Chain Length:197
Number of Molecules:6
Biological Source:Enterobacter
Ligand Molecules
Primary Citation
Structure-function analysis of the bacterial ClpE/ClpP AAA+ protease.
J. Biol. Chem. ? 111403 111403 (2026)
PMID: 41895441 DOI: 10.1016/j.jbc.2026.111403
Primary Citation of related structures
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