› 2hzy

X-ray diffraction
1.35Å resolution

Mouse fumarylacetoacetate hydrolase complexes with a transition-state mimic of the complete substrate

Released:
DOI: 10.2210/pdb2hzy/pdb
PDB entry 2hzy coloured by chain, front view.
PDB entry 2hzy coloured by chain, side view.
PDB entry 2hzy coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Slow-onset inhibition of fumarylacetoacetate hydrolase by phosphinate mimics of the tetrahedral intermediate: kinetics, crystal structure and pharmacokinetics.
Bateman RL, Ashworth J, Witte JF, Baker LJ, Bhanumoorthy P, Timm DE, Hurley TD, Grompe M, McClard RW
Biochem J 402 251-60 (2007)
PMID: 17064256

Function and Biology Details

Reaction catalysed: 
4-fumarylacetoacetate + H(2)O = acetoacetate + fumarate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152933 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fumarylacetoacetase Chains: A, B
Molecule details ›
Chains: A, B
Length: 421 amino acids
Theoretical weight: 46.3 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P35505 (Residues: 1-419; Coverage: 100%)
Gene name: Fah
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand NA 2 x NA
Ligand MN 2 x MN
Ligand CA 1 x CA
Ligand NI 10 x NI
Ligand DHJ 2 x DHJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 64.144Å b: 109.472Å c: 67.491Å
α: 90° β: 102.35° γ: 90°
R-values:
R R work R free
0.169 0.168 0.188
Expression system: Escherichia coli BL21

Quick links

Citations

9 citation in other articles

A universal system to select gene-modified hepatocytes in vivo.
Nygaard et al. (2016)
8 more

2 mentions without citation

Development and biological applications of sulfur-triazole exchange (SuTEx) chemistry.
Borne et al. (2021)
1 more