3KXP: Crystal Structure of E-2-(Acetamidomethylene)succinate Hydrolase

The gene identification and kinetic characterization of (E)-2-(acetamidomethylene)succinate (E-2AMS) hydrolase has recently been described. This enzyme catalyzes the final reaction in the degradation of vitamin B(6) and produces succinic semialdehyde, acetate, ammonia, and carbon dioxide from E-2AMS. The structure of E-2AMS hydrolase was determined to 2.3 A using SAD phasing. E-2AMS hydrolase is a member of the alpha/beta hydrolase superfamily and utilizes a serine/histidine/aspartic acid catalytic triad. Mutation of either the nucleophilic serine or the aspartate resulted in inactive enzyme. Mutation of an additional serine residue in the active site causes the enzyme to be unstable and is likely structurally important. The structure also provides insight into the mechanism of hydrolysis of E-2AMS and identifies several potential catalytically important residues.
PDB ID: 3KXPDownload
MMDB ID: 80002
PDB Deposition Date: 2009/12/3
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.26  Å
Source Organism:
Similar Structures:
Biological Unit for 3KXP: dimeric; determined by author and by software (PISA)
Molecular Components in 3KXP
Label Count Molecule
Proteins (2 molecules)
Alpha-(n-acetylaminomethylene)succinic Acid Hydrolase
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB