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 | 110 |
Details | Domain: {"description":"Plastocyanin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 65 |
Details | Domain: {"description":"Plastocyanin-like 2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"description":"type 2 copper site","evidences":[{"source":"PubMed","id":"11867755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12794077","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17217912","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17804014","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21903583","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24598746","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KV7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1N68","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PF3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FQE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FQF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FQG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YXV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YXW","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | Binding site: {"description":"type 3 copper site","evidences":[{"source":"PubMed","id":"11867755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12794077","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17217912","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17804014","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21903583","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24598746","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KV7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1N68","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PF3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FQD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FQE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FQF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FQG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YXV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YXW","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Binding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"11867755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12794077","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17217912","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17804014","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21903583","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24598746","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KV7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1N68","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PF3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FQD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FQE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FQF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FQG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YXV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YXW","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a65 |
Chain | Residue | Details |
A | CYS500 | |
A | HIS499 | |
A | HIS501 |