› 1m1t

X-ray diffraction
1.94Å resolution

Biosynthetic thiolase, Q64A mutant

Released:
DOI: 10.2210/pdb1m1t/pdb
PDB entry 1m1t coloured by chain, front view.
PDB entry 1m1t coloured by chain, side view.
PDB entry 1m1t coloured by chain, top view.
Source organism: Zoogloea ramigera
Primary publication:
The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes.
Kursula P, Ojala J, Lambeir AM, Wierenga RK
Biochemistry 41 15543-56 (2002)
PMID: 12501183

Function and Biology Details

Reaction catalysed: 
(1a) acetyl-CoA + [acetyl-CoA C-acetyltransferase]-L-cysteine = [acetyl-CoA C-acetyltransferase]-S-acetyl-L-cysteine + CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139369 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl-CoA acetyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 392 amino acids
Theoretical weight: 40.48 KDa
Source organism: Zoogloea ramigera
Expression system: Escherichia coli
UniProt:
  • Canonical: P07097 (Residues: 2-10, 11-392; Coverage: 100%)
Gene names: phaA, phbA
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21
Unit cell:
a: 84.47Å b: 78.953Å c: 148.291Å
α: 90° β: 92.55° γ: 90°
R-values:
R R work R free
0.201 0.199 0.245
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Ubiquitin: structures, functions, mechanisms.
Pickart et al. (2004)
3 more