› 5cmo

X-ray diffraction
2Å resolution

Crystal structure of holo-[acyl-carrier-protein] synthase (AcpS) from Neisseria meningitidis

Released:
DOI: 10.2210/pdb5cmo/pdb
PDB entry 5cmo coloured by chain, front view.
PDB entry 5cmo coloured by chain, side view.
PDB entry 5cmo coloured by chain, top view.
Source organism: Neisseria meningitidis FAM18
Entry authors: Nanson JD, Forwood JK

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:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106650 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Holo-[acyl-carrier-protein] synthase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 125 amino acids
Theoretical weight: 13.69 KDa
Source organism: Neisseria meningitidis FAM18
Expression system: Escherichia coli
UniProt:
  • Canonical: A1KVH5 (Residues: 1-125; Coverage: 100%)
Gene names: NMC1700, acpS
Sequence domains: 4'-phosphopantetheinyl transferase superfamily
Structure domains: 4'-phosphopantetheinyl transferase domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P212121
Unit cell:
a: 48.064Å b: 90.073Å c: 93.045Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.195 0.222
Expression system: Escherichia coli

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