1CC7
CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN
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 | 8 |
| Details | BINDING SITE FOR RESIDUE BEN A 186 |
| Chain | Residue |
| A | ILE4 |
| A | ASN23 |
| A | GLU30 |
| A | VAL33 |
| A | SER34 |
| A | ILE36 |
| A | LEU73 |
| A | HOH1001 |
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 |
