› 2c43

X-ray diffraction
1.93Å resolution

STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE- PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH COENZYME A

Released:
DOI: 10.2210/pdb2c43/pdb
PDB entry 2c43 coloured by chain, front view.
PDB entry 2c43 coloured by chain, side view.
PDB entry 2c43 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mechanism and substrate recognition of human holo ACP synthase.
Bunkoczi G, Pasta S, Joshi A, Wu X, Kavanagh KL, Smith S, Oppermann U
Chem Biol 14 1243-53 (2007)
PMID: 18022563

Function and Biology Details

Reaction catalysed: 
CoA-(4'-phosphopantetheine) + an apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + an [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-192565 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 37.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9NRN7 (Residues: 14-309; Coverage: 96%)
Gene names: AASDHPPT, CGI-80, HAH-P, HSPC223, x0005
Sequence domains: 4'-phosphopantetheinyl transferase superfamily
Structure domains: 4'-phosphopantetheinyl transferase domain

Ligands and Environments

3 bound ligands:
Ligand COA 1 x COA
Ligand MG 1 x MG
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 65.589Å b: 68.957Å c: 70.745Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.158 0.219
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Current understanding of fatty acid biosynthesis and the acyl carrier protein.
Chan et al. (2010)
8 more

6 mentions without citation

The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life.
Beld et al. (2014)
5 more