› 1bk4

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF RABBIT LIVER FRUCTOSE-1,6-BISPHOSPHATASE AT 2.3 ANGSTROM RESOLUTION

Released:
DOI: 10.2210/pdb1bk4/pdb
PDB entry 1bk4 coloured by chain, front view.
PDB entry 1bk4 coloured by chain, side view.
PDB entry 1bk4 coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 A resolution.
Weeks CM, Roszak AW, Erman M, Kaiser R, Jörnvall H, Ghosh D
Acta Crystallogr D Biol Crystallogr 55 93-102 (1999)
PMID: 10089399

Function and Biology Details

Reaction catalysed: 
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132779 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-1,6-bisphosphatase 1 Chain: A
Molecule details ›
Chain: A
Length: 337 amino acids
Theoretical weight: 36.49 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P00637 (Residues: 2-338; Coverage: 100%)
Gene names: FBP, FBP1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 73.79Å b: 80.05Å c: 131.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 not available

Quick links

Citations

7 citation in other articles

Hydrophobic complementarity in protein-protein docking.
Berchanski et al. (2004)
6 more

1 mention without citation

Most partial domains in proteins are alignment and annotation artifacts.
Triant et al. (2015)