3hln

X-ray diffraction
3.2Å resolution

Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds

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:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetradecamer (preferred)
PDBe Complex ID:
PDB-CPX-141326 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease proteolytic subunit Chains: 1, 2, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z
Molecule details ›
Chains: 1, 2, A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z
Length: 193 amino acids
Theoretical weight: 21.62 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6G7 (Residues: 15-207; Coverage: 93%)
Gene names: JW0427, b0437, clpP, lopP
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3221
Unit cell:
a: 182.299Å b: 182.299Å c: 476.859Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.213 0.253
Expression system: Escherichia coli