Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
9Q0 1-{5-[(1s)-2-amino-1-hydroxy-2-oxo-1-phenylethyl]-7,8-dimethyl-2,4-dioxo-1,2,3,4-tetrahydrobenzo[G]pteridine-5,10-diium-10-yl}-1-deoxy-5-O-phosphono-D-ribitol
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 6A3T   PDBj   RCSB PDB   PDBe
Header : FLAVOPROTEIN
Title : The crystal structure of Mandelate oxidase R163L with 2-hydroxy-phenylacetamide
Release Data : 2019-06-19
Compound :
mol_id molecule chains
1 4-hydroxymandelate oxidase A
ec: 1.1.3.46
mutation: R163L
Source :
mol_id organism_scientific organism_common expression_system
1 Amycolatopsis orientalis  (taxid:31958) Nocardia orientalis Escherichia coli  (taxid:562)
gene: hmo
Authors : Li, T.L., Lin, K.H.
Keywords : FMN-dependent oxidase, flavoprotein
Exp. method : X-RAY DIFFRACTION ( 2.511 Å )
Citation :

The flavin mononucleotide cofactor in alpha-hydroxyacid oxidases exerts its electrophilic/nucleophilic duality in control of the substrate-oxidation level.

Lyu, S.Y.,Lin, K.H.,Yeh, H.W.  et al.
(2019)  Acta Crystallogr D Struct Biol  75 : 918 - 929

PubMed: 31588923
DOI: 10.1107/S2059798319011938

Chain : A
UniProt : O52792 (HMO_AMYOR)
Reaction: EC: Evidence:
Physiological Direction:
(S)-4-hydroxymandelate + O2 = 4-hydroxyphenylglyoxylate + H2O2 1.1.3.46 PubMed:11137816, PubMed:12240298
-