1kbr

X-ray diffraction
1.55Å resolution

CRYSTAL STRUCTURE OF UNLIGATED HPPK(R92A) FROM E.COLI AT 1.55 ANGSTROM RESOLUTION

Released:

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: 17.88 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
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

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P21
Unit cell:
a: 36.34Å b: 46.943Å c: 42.907Å
α: 90° β: 110.49° γ: 90°
R-values:
R R work R free
0.192 0.168 0.208
Expression system: Escherichia coli BL21(DE3)