1FES
SOLUTION STRUCTURE OF THE APO 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 | 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 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 | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00280, ECO:0000269|PubMed:11327811, ECO:0000269|PubMed:19965379, ECO:0000269|PubMed:28865724, ECO:0007744|PDB:1FD8, ECO:0007744|PDB:3K7R, ECO:0007744|PDB:5VDE, ECO:0007744|PDB:5VDF |
Chain | Residue | Details |
A | CYS15 | |
A | CYS18 |