› 4xvx

X-ray diffraction
2.3Å resolution

Crystal structure of an acyl-ACP dehydrogenase

Released:
DOI: 10.2210/pdb4xvx/pdb
PDB entry 4xvx coloured by chain, front view.
PDB entry 4xvx coloured by chain, side view.
PDB entry 4xvx coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
A covalent adduct of MbtN, an acyl-ACP dehydrogenase from Mycobacterium tuberculosis, reveals an unusual acyl-binding pocket.
Chai AF, Bulloch EM, Evans GL, Lott JS, Baker EN, Johnston JM
Acta Crystallogr D Biol Crystallogr 71 862-72 (2015)
PMID: 25849397

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162073 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-[acyl-carrier-protein] dehydrogenase MbtN Chains: A, B
Molecule details ›
Chains: A, B
Length: 389 amino acids
Theoretical weight: 41.42 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WQF9 (Residues: 2-386; Coverage: 100%)
Gene names: MTCY02B10.10, Rv1346, fadE14, mbtN
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand P33 1 x P33
Ligand FDA 2 x FDA
Ligand P6G 1 x P6G
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: R32
Unit cell:
a: 139.104Å b: 139.104Å c: 253.093Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.175 0.212
Expression system: Escherichia coli BL21(DE3)

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Citations

3 citation in other articles

Mycobacteria Tolerate Carbon Monoxide by Remodeling Their Respiratory Chain.
Bayly et al. (2021)
2 more