TABLE 1.
Sequence alignment between LCCI, LCCIa, 1a65, and zAO
| Protein | Sequence alignmenta |
|---|---|
| LCCI | 471LHCHIDFHLD AGFAIVFAED VADVKAANPV PKAWSDLCPI YDGLSEANQ519 |
| LCCIa | 471LHCHIDFHLD AGFAIVFAED VADVKAANPV PKAWSDLCC509 |
| 1a65 | 450FHCHIEFHLM NGLAIVFAED MANTVDANNP PVEWAQLCEI YDDLPPEATS IQTTV504 |
| 1AOZ | 505FHCHIEPHLH MGMGVVFAEG VEKVGRIPTK ALACGGTAKS LINNPKNP552 |
| Cu-type | 31311 |
a
Residues in boldface type highlight the differences between LCCI and LCCIa. Underlined residues are ligands (coordinated or in close proximity) to type-1 and type-3 copper ions. Cysteine residues that are double-underlined are involved in formation of a disulfide bridge. 1a65 and zAO correspond to the crystal structures of laccase (Coprinus cinereus) and ascorbate oxidase (Cucurbita pepo medullosa), respectively, available through the Protein Data Bank (17, 30).