3kug

X-ray diffraction
2Å resolution

Crystal structure of E. coli HPPK(H115A)

Released:
Source organism: Escherichia coli K-12
Entry authors: Blaszczyk J, Li Y, Yan H, Ji X

Function and Biology Details

Reaction catalysed:
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8-dihydropterin diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 17.9 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P26281 (Residues: 2-159; Coverage: 99%)
Gene names: JW0138, b0142, folK
Sequence domains: 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK)
Structure domains: 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P21
Unit cell:
a: 36.1Å b: 47Å c: 42.2Å
α: 90° β: 114.5° γ: 90°
R-values:
R R work R free
0.197 0.192 0.233
Expression system: Escherichia coli