› 3fla

X-ray diffraction
1.8Å resolution

RifR - Type II thioesterase from Rifamycin NRPS/PKS biosynthetic pathway - Form 1

Released:
DOI: 10.2210/pdb3fla/pdb
PDB entry 3fla coloured by chain, front view.
PDB entry 3fla coloured by chain, side view.
PDB entry 3fla coloured by chain, top view.
Source organism: Amycolatopsis mediterranei
Primary publication:
Structure and functional analysis of RifR, the type II thioesterase from the rifamycin biosynthetic pathway.
Claxton HB, Akey DL, Silver MK, Admiraal SJ, Smith JL
J Biol Chem 284 5021-9 (2009)
PMID: 19103602

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181381 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polyketide synthase thioesterase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 267 amino acids
Theoretical weight: 29.61 KDa
Source organism: Amycolatopsis mediterranei
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7BUF9 (Residues: 1-259; Coverage: 100%)
Gene name: rifR
Sequence domains: Thioesterase domain
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand CL 2 x CL
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 39.507Å b: 94.648Å c: 63.174Å
α: 90° β: 90.55° γ: 90°
R-values:
R R work R free
0.174 0.172 0.202
Expression system: Escherichia coli

Quick links

Citations

4 review citations

PKS and NRPS release mechanisms.
Du et al. (2010)
3 more

8 mentions without citation

Thioesterases: a new perspective based on their primary and tertiary structures.
Cantu et al. (2010)
7 more