› 2g1h

X-ray diffraction
1.86Å resolution

Structure of E.coli FabD complexed with glycerol

Released:
DOI: 10.2210/pdb2g1h/pdb
PDB entry 2g1h coloured by chain, front view.
PDB entry 2g1h coloured by chain, side view.
PDB entry 2g1h coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Mapping the active site of Escherichia coli malonyl-CoA-acyl carrier protein transacylase (FabD) by protein crystallography.
Oefner C, Schulz H, D'Arcy A, Dale GE
Acta Crystallogr D Biol Crystallogr 62 613-8 (2006)
PMID: 16699188

Function and Biology Details

Reaction catalysed: 
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141990 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malonyl CoA-acyl carrier protein transacylase Chain: A
Molecule details ›
Chain: A
Length: 308 amino acids
Theoretical weight: 32.31 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AAI9 (Residues: 2-309; Coverage: 100%)
Gene names: JW1078, b1092, fabD, tfpA
Sequence domains: Acyl transferase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P41212
Unit cell:
a: 83.147Å b: 83.147Å c: 164.511Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.222
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Chemistry and biology of multicomponent reactions.
Dömling et al. (2012)
10 more

4 mentions without citation

Fatty acid biosynthesis revisited: structure elucidation and metabolic engineering.
Beld et al. (2015)
3 more