7fep

Electron Microscopy
3.1Å resolution

Cryo-EM structure of BsClpP-ADEP1 complex at pH 6.5

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero 28-mer (preferred)
PDBe Complex ID:
PDB-CPX-160371 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent Clp protease proteolytic subunit Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 202 amino acids
Theoretical weight: 22.4 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
ADEP1 Chains: O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b
Molecule details ›
Chains: O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b
Length: 7 amino acids
Theoretical weight: 737 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
2 modified residues:

Experiments and Validation Details

Entry percentile scores
Resolution: 3.1Å
Relevant EMDB volumes: EMD-31559
Expression systems:
  • Escherichia coli
  • Not provided