› 5o0b

X-ray diffraction
1.74Å resolution

Crystal structure of Phosphopantetheine adenylyltransferase from Mycobacterium abcessus in complex with 3-Bromo-1H-indazole-5-carboxylic acid (Fragment 2)

Released:
DOI: 10.2210/pdb5o0b/pdb
PDB 5o0b coloured by chain and viewed from the front.
PDB 5o0b coloured by chain and viewed from the side.
PDB 5o0b coloured by chain and viewed from the top.
Source organism: Mycobacteroides abscessus ATCC 19977
Primary publication:
Structural biology and the design of new therapeutics: from HIV and cancer to mycobacterial infections.
Thomas SE, Mendes V, Kim SY, Malhotra S, Ochoa-Montaño B, Blaszczyk M, Blundell TL
J. Mol. Biol. (2017)
PMID: 28648615

Function and Biology Details

Reaction catalysed: 
ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphopantetheine adenylyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 162 amino acids
Theoretical weight: 17.48 KDa
Source organism: Mycobacteroides abscessus ATCC 19977
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B1MDL6 (Residues: 1-161; Coverage: 100%)
Gene names: MAB_3259c, coaD
Sequence domains: Cytidylyltransferase-like
Structure domains: HUPs

Ligands and Environments

1 bound ligand:
Ligand 9FE 6 x 9FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: C2221
Unit cell:
a: 76.069Å b: 125.171Å c: 119.435Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.198 0.229
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Fragment-Based Drug Discovery against Mycobacteria: The Success and Challenges.
Togre et al. (2022)
4 more

1 mention without citation

Structural Characterization of Mycobacterium abscessus Phosphopantetheine Adenylyl Transferase Ligand Interactions: Implications for Fragment-Based Drug Design.
Thomas et al. (2022)