1FD8
SOLUTION STRUCTURE OF THE CU(I) FORM OF THE YEAST METALLOCHAPERONE, ATX1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0006825 | biological_process | copper ion transport |
A | 0006879 | biological_process | intracellular iron ion homeostasis |
A | 0016531 | molecular_function | copper chaperone activity |
A | 0034599 | biological_process | cellular response to oxidative stress |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU1 A 74 |
Chain | Residue |
A | THR14 |
A | CYS15 |
A | CYS18 |
A | LYS65 |
Functional Information from PROSITE/UniProt
site_id | PS01047 |
Number of Residues | 31 |
Details | HMA_1 Heavy-metal-associated domain. NvVMtCsGCsgaVNkvLtklepdvskidIsL |
Chain | Residue | Details |
A | ASN10-LEU40 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 64 |
Details | Domain: {"description":"HMA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00280","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00280","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11327811","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19965379","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28865724","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FD8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K7R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5VDE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5VDF","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |