2H5U
Crystal structure of laccase from Cerrena maxima at 1.9A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046274 | biological_process | lignin catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052716 | molecular_function | hydroquinone:oxygen oxidoreductase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00079 |
| Number of Residues | 21 |
| Details | MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GtFwYhShLStqYcDGLrgpF |
| Chain | Residue | Details |
| A | GLY104-PHE124 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: type 2 copper site => ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV |
| Chain | Residue | Details |
| A | HIS64 | |
| A | HIS398 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: type 3 copper site => ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV |
| Chain | Residue | Details |
| A | HIS66 | |
| A | HIS109 | |
| A | HIS111 | |
| A | HIS400 | |
| A | HIS452 | |
| A | HIS454 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: type 1 copper site => ECO:0000269|PubMed:16944230, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV |
| Chain | Residue | Details |
| A | HIS395 | |
| A | CYS453 | |
| A | HIS458 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: 3'-nitrotyrosine => ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782, ECO:0000269|Ref.3 |
| Chain | Residue | Details |
| A | NIY196 | |
| A | NIY372 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 5 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN51 | |
| A | ASN208 | |
| A | ASN292 | |
| A | ASN377 | |
| A | ASN416 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U |
| Chain | Residue | Details |
| A | ASN54 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782, ECO:0000269|Ref.3, ECO:0007744|PDB:2H5U, ECO:0007744|PDB:3DIV |
| Chain | Residue | Details |
| A | ASN217 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16944230, ECO:0007744|PDB:2H5U |
| Chain | Residue | Details |
| A | ASN333 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16944230, ECO:0000269|PubMed:17012782, ECO:0007744|PDB:2H5U |
| Chain | Residue | Details |
| A | ASN436 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a65 |
| Chain | Residue | Details |
| A | HIS452 | |
| A | HIS454 | |
| A | CYS453 |
