› 4wd1

X-ray diffraction
1.9Å resolution

Acetoacetyl-CoA Synthetase from Streptomyces lividans

Released:
DOI: 10.2210/pdb4wd1/pdb
PDB entry 4wd1 coloured by chain, front view.
PDB entry 4wd1 coloured by chain, side view.
PDB entry 4wd1 coloured by chain, top view.
Source organism: Streptomyces lividans TK24
Primary publication:
The structure of S. lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain.
Mitchell CA, Tucker AC, Escalante-Semerena JC, Gulick AM
Proteins 83 575-81 (2015)
PMID: 25488501

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112776 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetoacetate-CoA ligase Chain: A
Molecule details ›
Chain: A
Length: 658 amino acids
Theoretical weight: 72.33 KDa
Source organism: Streptomyces lividans TK24
Expression system: Escherichia coli
UniProt:
  • Canonical: D6EQU8 (Residues: 1-658; Coverage: 100%)
Gene name: SSPG_06161
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand EDO 22 x EDO
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P3121
Unit cell:
a: 104.408Å b: 104.408Å c: 133.906Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.162 0.16 0.194
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress.
Hentchel et al. (2015)
2 other articles

4 mentions without citation

Inherent dynamics of head domain correlates with ATP-recognition of P2X4 receptors: insights gained from molecular simulations.
Huang et al. (2014)
3 more