2FQE
Crystal Structures of E. coli Laccase CueO under different copper binding situations
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004322 | molecular_function | ferroxidase activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0010273 | biological_process | detoxification of copper ion |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016682 | molecular_function | oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor |
| A | 0016722 | molecular_function | oxidoreductase activity, acting on metal ions |
| A | 0016724 | molecular_function | oxidoreductase activity, acting on metal ions, oxygen as acceptor |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046688 | biological_process | response to copper ion |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 601 |
| Chain | Residue |
| A | LEU442 |
| A | HIS443 |
| A | CYS500 |
| A | HIS505 |
| A | MET510 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CU A 603 |
| Chain | Residue |
| A | C2O602 |
| A | HOH907 |
| A | HIS101 |
| A | HIS103 |
| A | HIS446 |
| A | HIS448 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 901 |
| Chain | Residue |
| A | LYS124 |
| A | GLU266 |
| A | ASP332 |
| A | HOH1191 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE C2O A 602 |
| Chain | Residue |
| A | HIS101 |
| A | HIS103 |
| A | TRP139 |
| A | HIS141 |
| A | HIS143 |
| A | HIS446 |
| A | HIS448 |
| A | HIS499 |
| A | HIS501 |
| A | CU603 |
| A | HOH1097 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CIT A 701 |
| Chain | Residue |
| A | ARG45 |
| A | ARG82 |
| A | PRO134 |
| A | TRP469 |
| A | LYS485 |
| A | ASN487 |
| A | HOH928 |
| A | HOH1001 |
| A | HOH1114 |
| A | HOH1122 |
Functional Information from PROSITE/UniProt
| site_id | PS00080 |
| Number of Residues | 12 |
| Details | MULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHlleHedtGM |
| Chain | Residue | Details |
| A | HIS499-MET510 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: type 2 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW |
| Chain | Residue | Details |
| A | HIS101 | |
| A | HIS446 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: type 3 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW |
| Chain | Residue | Details |
| A | HIS103 | |
| A | HIS141 | |
| A | HIS143 | |
| A | HIS448 | |
| A | HIS499 | |
| A | HIS501 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: type 1 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW |
| Chain | Residue | Details |
| A | HIS443 | |
| A | CYS500 | |
| A | HIS505 |
