› 2f99

X-ray diffraction
1.9Å resolution

Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: implications for catalytic mechanism and product stereoselectivity.

Released:
DOI: 10.2210/pdb2f99/pdb
PDB entry 2f99 coloured by chain, front view.
PDB entry 2f99 coloured by chain, side view.
PDB entry 2f99 coloured by chain, top view.
Source organism: Streptomyces galilaeus
Primary publication:
Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: implications for catalytic mechanism and product stereoselectivity.
Kallio P, Sultana A, Niemi J, Mäntsälä P, Schneider G
J Mol Biol 357 210-20 (2006)
PMID: 16414075

Function and Biology Details

Reaction catalysed: 
Aklaviketone = methyl aklanonate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129397 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aklanonic acid methyl ester cyclase AcmA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 153 amino acids
Theoretical weight: 17.95 KDa
Source organism: Streptomyces galilaeus
Expression system: Escherichia coli
UniProt:
  • Canonical: O52646 (Residues: 2-144; Coverage: 99%)
Gene names: acma, aknH
Sequence domains: SnoaL-like polyketide cyclase
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

2 bound ligands:
Ligand SO4 11 x SO4
Ligand AKV 4 x AKV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: R3
Unit cell:
a: 151.74Å b: 151.74Å c: 108.868Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.185 0.207
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Biosynthesis of polyketides by trans-AT polyketide synthases.
Helfrich et al. (2016)
5 more

3 mentions without citation

An enumerative algorithm for de novo design of proteins with diverse pocket structures.
Basanta et al. (2020)
2 more