› 7kr2

Electron Microscopy
3.2Å resolution

ClpP from Neisseria meningitidis - Compressed conformation

Released:
DOI: 10.2210/pdb7kr2/pdb
PDB entry 7kr2 coloured by chain, front view.
PDB entry 7kr2 coloured by chain, side view.
PDB entry 7kr2 coloured by chain, top view.
Source organism: Neisseria meningitidis
Entry authors: Ripstein ZA, Vahidi S, Rubinstein JL, Kay LE
Related structures: EMD-23000

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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetradecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191701 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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: 204 amino acids
Theoretical weight: 22.7 KDa
Source organism: Neisseria meningitidis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9JZ38 (Residues: 1-204; Coverage: 100%)
Gene names: NMB1312, clpP
Sequence domains: Clp protease

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.2Å
Relevant EMDB volumes: EMD-23000
Expression system: Escherichia coli BL21(DE3)

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