3PAU
CueO in the resting oxidized state
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 | 8 |
Details | BINDING SITE FOR RESIDUE C2O A 701 |
Chain | Residue |
A | HIS103 |
A | HIS141 |
A | HIS143 |
A | HIS448 |
A | HIS499 |
A | HIS501 |
A | HOH692 |
A | CU801 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CU A 801 |
Chain | Residue |
A | HIS103 |
A | HIS446 |
A | HIS448 |
A | HOH691 |
A | C2O701 |
A | HIS101 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU A 802 |
Chain | Residue |
A | LEU442 |
A | HIS443 |
A | CYS500 |
A | HIS505 |
A | MET510 |
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 |