› 4jv3

X-ray diffraction
1.7Å resolution

Crystal structure of beta-ketoacyl synthase from Brucella melitensis in complex with platencin

Released:
DOI: 10.2210/pdb4jv3/pdb
PDB entry 4jv3 coloured by chain, front view.
PDB entry 4jv3 coloured by chain, side view.
PDB entry 4jv3 coloured by chain, top view.
Source organism: Brucella abortus 2308
Primary publication:
Structural characterization of β-ketoacyl ACP synthase I bound to platencin and fragment screening molecules at two substrate binding sites.
Patterson EI, Nanson JD, Abendroth J, Bryan C, Sankaran B, Myler PJ, Forwood JK
Proteins 88 47-56 (2020)
PMID: 31237717

Function and Biology Details

Reaction catalysed: 
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174196 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] synthase 1 Chain: A
Molecule details ›
Chain: A
Length: 428 amino acids
Theoretical weight: 45.72 KDa
Source organism: Brucella abortus 2308
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q2YQQ9 (Residues: 1-407; Coverage: 100%)
Gene names: BAB1_2173, fabB
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

1 bound ligand:
Ligand N32 1 x N32
1 modified residue:
Ligand CSU 1 x CSU

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 78.16Å b: 84.48Å c: 74.02Å
α: 90° β: 120.81° γ: 90°
R-values:
R R work R free
0.144 0.142 0.169
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Application of Fragment-Based Drug Discovery to Versatile Targets.
Li Q. (2020)

2 mentions without citation

Structural characterization of β-ketoacyl ACP synthase I bound to platencin and fragment screening molecules at two substrate binding sites.
Patterson et al. (2020)
1 more