3mt6

X-ray diffraction
1.9Å resolution

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:
hetero 28-mer (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, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b
Molecule details ›
Chains: 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, a, b
Length: 207 amino acids
Theoretical weight: 23.21 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6G7 (Residues: 1-207; Coverage: 100%)
Gene names: JW0427, b0437, clpP, lopP
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1
ACYLDEPSIPEPTIDE 1 Chains: 1, 2, 3, 4, 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, 3, 4, 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: 7 amino acids
Theoretical weight: 737 Da
Source organism: Streptomyces hawaiiensis

Ligands and Environments

1 bound ligand:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 93.254Å b: 121.15Å c: 276.17Å
α: 90° β: 91.38° γ: 90°
R-values:
R R work R free
0.178 0.178 0.204
Expression system: Escherichia coli