2bmb

X-ray diffraction
2.3Å resolution

X-ray structure of the bifunctional 6-hydroxymethyl-7,8- dihydroxypterin pyrophosphokinase dihydropteroate synthase from Saccharomyces cerevisiae

Released:

Function and Biology Details

Reactions catalysed:
7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Folic acid synthesis protein FOL1 Chain: A
Molecule details ›
Chain: A
Length: 545 amino acids
Theoretical weight: 61.7 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P53848 (Residues: 293-824; Coverage: 65%)
Gene names: FOL1, N0848, YNL256W
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P41212
Unit cell:
a: 92.566Å b: 92.566Å c: 192.401Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.216
Expression system: Escherichia coli BL21(DE3)