5F0W
Crystal structure of human copper homeostatic proteins atox1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006825 | biological_process | copper ion transport |
| A | 0006878 | biological_process | intracellular copper ion homeostasis |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0016530 | molecular_function | metallochaperone activity |
| A | 0016531 | molecular_function | copper chaperone activity |
| A | 0032767 | molecular_function | copper-dependent protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1903136 | molecular_function | cuprous ion binding |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006825 | biological_process | copper ion transport |
| B | 0006878 | biological_process | intracellular copper ion homeostasis |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0016530 | molecular_function | metallochaperone activity |
| B | 0016531 | molecular_function | copper chaperone activity |
| B | 0032767 | molecular_function | copper-dependent protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1903136 | molecular_function | cuprous ion binding |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006825 | biological_process | copper ion transport |
| C | 0006878 | biological_process | intracellular copper ion homeostasis |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0016530 | molecular_function | metallochaperone activity |
| C | 0016531 | molecular_function | copper chaperone activity |
| C | 0032767 | molecular_function | copper-dependent protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1903136 | molecular_function | cuprous ion binding |
| D | 0005507 | molecular_function | copper ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006825 | biological_process | copper ion transport |
| D | 0006878 | biological_process | intracellular copper ion homeostasis |
| D | 0006979 | biological_process | response to oxidative stress |
| D | 0016530 | molecular_function | metallochaperone activity |
| D | 0016531 | molecular_function | copper chaperone activity |
| D | 0032767 | molecular_function | copper-dependent protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1903136 | molecular_function | cuprous ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue AG A 101 |
| Chain | Residue |
| A | GLY14 |
| A | CYS15 |
| A | LYS60 |
| A | AG102 |
| A | HOH203 |
| B | THR11 |
| B | CYS12 |
| B | AG102 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue AG A 102 |
| Chain | Residue |
| A | CYS12 |
| A | CYS15 |
| A | AG101 |
| B | CYS12 |
| B | AG101 |
| B | AG102 |
| A | THR11 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue AG B 101 |
| Chain | Residue |
| A | THR11 |
| A | CYS12 |
| A | AG102 |
| B | GLY14 |
| B | CYS15 |
| B | LYS60 |
| B | AG102 |
| B | HOH202 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue AG B 102 |
| Chain | Residue |
| A | CYS12 |
| A | AG101 |
| A | AG102 |
| B | THR11 |
| B | CYS12 |
| B | CYS15 |
| B | AG101 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue AG C 101 |
| Chain | Residue |
| C | GLY14 |
| C | CYS15 |
| C | AG102 |
| D | THR11 |
| D | CYS12 |
| D | AG102 |
| D | HOH202 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue AG C 102 |
| Chain | Residue |
| C | THR11 |
| C | CYS12 |
| C | CYS15 |
| C | AG101 |
| D | CYS12 |
| D | AG101 |
| D | AG102 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue AG D 101 |
| Chain | Residue |
| C | THR11 |
| C | CYS12 |
| C | AG102 |
| D | GLY14 |
| D | CYS15 |
| D | LYS60 |
| D | AG102 |
| D | HOH203 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue AG D 102 |
| Chain | Residue |
| C | CYS12 |
| C | AG101 |
| C | AG102 |
| D | THR11 |
| D | CYS12 |
| D | CYS15 |
| D | AG101 |
Functional Information from PROSITE/UniProt
| site_id | PS01047 |
| Number of Residues | 29 |
| Details | HMA_1 Heavy-metal-associated domain. SvDMtCgGCaeaVSrvLnklggvkyd..IdL |
| Chain | Residue | Details |
| A | SER7-LEU35 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00280, ECO:0000269|PubMed:31283225, ECO:0007744|PDB:5T7L |
| Chain | Residue | Details |
| A | CYS12 | |
| A | CYS15 | |
| B | CYS12 | |
| B | CYS15 | |
| C | CYS12 | |
| C | CYS15 | |
| D | CYS12 | |
| D | CYS15 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER47 | |
| B | SER47 | |
| C | SER47 | |
| D | SER47 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O08997 |
| Chain | Residue | Details |
| A | LYS60 | |
| B | LYS60 | |
| C | LYS60 | |
| D | LYS60 |
