Multicopper oxidase

Multicopper oxidase (type 1)
crystal structures of e. coli laccase cueo under different copper binding situations
Identifiers
Symbol	Cu-oxidase
Pfam	PF00394
Pfam clan	CL0026
InterPro	IPR001117
PROSITE	PDOC00076
SCOP	1aoz
SUPERFAMILY	1aoz
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Multicopper oxidase (type 2)
active laccase from trametes versicolor complexed with 2,5-xylidine
Identifiers
Symbol	Cu-oxidase_2
Pfam	PF07731
Pfam clan	CL0026
InterPro	IPR011706
SCOP	1aoz
SUPERFAMILY	1aoz
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Multicopper oxidase (type 3)
crystal structures of e. coli laccase cueo under different copper binding situations
Identifiers
Symbol	Cu-oxidase_3
Pfam	PF07732
Pfam clan	CL0026
InterPro	IPR011707
SCOP	1aoz
SUPERFAMILY	1aoz
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

CMulti-copper polyphenol oxidoreductase laccase
crystal structure of protein cc_0490 from caulobacter crescentus, pfam duf152
Identifiers
Symbol	Cu-oxidase_4
Pfam	PF02578
InterPro	IPR003730
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In molecular biology, multicopper oxidases are enzymes which oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre; dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water. There are three spectroscopically different copper centres found in multicopper oxidases: type 1 (or blue), type 2 (or normal) and type 3 (or coupled binuclear). Multicopper oxidases consist of 2, 3 or 6 of these homologous domains, which also share homology with the cupredoxins azurin and . Structurally, these domains consist of a cupredoxin-like fold, a beta-sandwich consisting of 7 strands in 2 beta-sheets, arranged in a Greek-key beta-barrel. Multicopper oxidases include:

In addition to the above enzymes there are a number of other proteins that are similar to the multi-copper oxidases in terms of structure and sequence, some of which have lost the ability to bind copper. These include: copper resistance protein A (copA) from a plasmid in Pseudomonas syringae; domain A of (non-copper binding) blood coagulation factors V (Fa V) and VIII (Fa VIII);yeast Fet3p (FET3) required for ferrous iron uptake;yeast hypothetical protein YFL041w; and the fission yeast homologue SpAC1F7.08.