› 1im6

X-ray diffraction
1.74Å resolution

CRYSTAL STRUCTURE OF UNLIGATED HPPK(R82A) FROM E.COLI AT 1.74 ANGSTROM RESOLUTION

Released:
DOI: 10.2210/pdb1im6/pdb
PDB entry 1im6 coloured by chain, front view.
PDB entry 1im6 coloured by chain, side view.
PDB entry 1im6 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Dynamic roles of arginine residues 82 and 92 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: crystallographic studies.
Blaszczyk J, Li Y, Shi G, Yan H, Ji X
Biochemistry 42 1573-80 (2003)
PMID: 12578370

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150686 (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:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P21
Unit cell:
a: 36.106Å b: 47.178Å c: 43.816Å
α: 90° β: 109.44° γ: 90°
R-values:
R R work R free
0.191 0.172 0.206
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Folate biosynthesis pathway: mechanisms and insights into drug design for infectious diseases.
Bertacine Dias et al. (2018)
1 more

1 mention without citation

BUDDY-system: A web site for constructing a dataset of protein pairs between ligand-bound and unbound states.
Morita et al. (2011)