2zle

Electron Microscopy
28Å resolution

Cryo-EM structure of DegP12/OMP

Released:
Source organism: Escherichia coli
Related structures: EMD-1505

Function and Biology Details

Reaction catalysed:
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tridecamer (preferred)
PDBe Complex ID:
PDB-CPX-139327 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Periplasmic serine endoprotease DegP Chains: A, B, C, E, F, G, H, I, J, K, L, M
Molecule details ›
Chains: A, B, C, E, F, G, H, I, J, K, L, M
Length: 448 amino acids
Theoretical weight: 46.87 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C0V0 (Residues: 27-474; Coverage: 100%)
Gene names: JW0157, b0161, degP, htrA, ptd
Sequence domains:
Outer membrane porin C Chain: D
Molecule details ›
Chain: D
Length: 346 amino acids
Theoretical weight: 38.34 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P06996 (Residues: 22-367; Coverage: 100%)
Gene names: JW2203, b2215, meoA, ompC, par
Sequence domains: Gram-negative porin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 28Å
Relevant EMDB volumes: EMD-1505
Expression system: Escherichia coli