› 3ix1

X-ray diffraction
2.4Å resolution

Periplasmic N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine binding protein from Bacillus halodurans

Released:
DOI: 10.2210/pdb3ix1/pdb
PDB entry 3ix1 coloured by chain, front view.
PDB entry 3ix1 coloured by chain, side view.
PDB entry 3ix1 coloured by chain, top view.
Source organism: Alkalihalobacillus halodurans C-125
Primary publication:
HMP binding protein ThiY and HMP-P synthase THI5 are structural homologues.
Bale S, Rajashankar KR, Perry K, Begley TP, Ealick SE
Biochemistry 49 8929-36 (2010)
PMID: 20873853

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191793 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formylaminopyrimidine-binding protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 302 amino acids
Theoretical weight: 33.31 KDa
Source organism: Alkalihalobacillus halodurans C-125
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9K9G5 (Residues: 29-330; Coverage: 97%)
Gene names: BH2682, thiY
Sequence domains: NMT1/THI5 like
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

1 bound ligand:
Ligand NFM 2 x NFM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 59.918Å b: 96.953Å c: 104.888Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.264
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Diversity of membrane transport proteins for vitamins in bacteria and archaea.
Jaehme et al. (2015)
8 other articles

4 mentions without citation

Accurate macromolecular crystallographic refinement: incorporation of the linear scaling, semiempirical quantum-mechanics program DivCon into the PHENIX refinement package.
Borbulevych et al. (2014)
3 more