3CJK
Crystal structure of the adduct HAH1-Cd(II)-MNK1.
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 | 0006811 | biological_process | monoatomic ion transport |
| 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 | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051117 | molecular_function | ATPase binding |
| A | 0060003 | biological_process | copper ion export |
| A | 1903136 | molecular_function | cuprous ion binding |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD B 1 |
| Chain | Residue |
| A | CYS12 |
| B | THR14 |
| B | CYS15 |
| B | CYS18 |
Functional Information from PROSITE/UniProt
| site_id | PS01047 |
| Number of Residues | 30 |
| Details | HMA_1 Heavy-metal-associated domain. VeGMtCnSCvwtIEqqIgkvngvhhik.VsL |
| Chain | Residue | Details |
| B | VAL10-LEU39 | |
| A | SER7-LEU35 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00280","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31283225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5T7L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O08997","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 66 |
| Details | Domain: {"description":"HMA 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00280","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31283225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5T7L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
