Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.1
Classification:OXIDOREDUCTASE
Release Date:2006-10-23
Deposition Date:2006-10-05
Revision Date:2011-05-08#2011-07-13
Molecular Weight:330986.28
Macromolecule Type:Protein
Residue Count:2992
Atom Site Count:22565
DOI:10.2210/pdb2j6x/pdb
Abstract:
The crystal structure of L-lactate oxidase (LOX) from Aerococcus viridans has been determined at 2.1 A resolution. LOX catalyzes the flavin mononucleotide (FMN) dependent oxidation of lactate to pyruvate and hydrogen peroxide. LOX belongs to the alpha-hydroxy-acid oxidase flavoenzyme family; members of which bind similar substrates and to some extent have conserved catalytic properties and structural motifs. LOX crystallized as two tightly packed tetramers in the asymmetric unit, each having fourfold symmetry. The present structure shows a conserved FMN coordination, but also reveals novel residues involved in substrate binding compared with other family members.
Resolution:2.1
Classification:OXIDOREDUCTASE
Release Date:2006-10-23
Deposition Date:2006-10-05
Revision Date:2011-05-08#2011-07-13
Molecular Weight:330986.28
Macromolecule Type:Protein
Residue Count:2992
Atom Site Count:22565
DOI:10.2210/pdb2j6x/pdb
Abstract:
The crystal structure of L-lactate oxidase (LOX) from Aerococcus viridans has been determined at 2.1 A resolution. LOX catalyzes the flavin mononucleotide (FMN) dependent oxidation of lactate to pyruvate and hydrogen peroxide. LOX belongs to the alpha-hydroxy-acid oxidase flavoenzyme family; members of which bind similar substrates and to some extent have conserved catalytic properties and structural motifs. LOX crystallized as two tightly packed tetramers in the asymmetric unit, each having fourfold symmetry. The present structure shows a conserved FMN coordination, but also reveals novel residues involved in substrate binding compared with other family members.
| Date made available | 2006 |
|---|---|
| Publisher | RCSB-PDB |