4QOT
Crystal structure of human copper chaperone bound to the platinum ion
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 | 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 | 0006811 | biological_process | monoatomic ion transport |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PT A 101 |
Chain | Residue |
A | CYS12 |
A | CYS15 |
B | CYS12 |
B | CYS15 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 102 |
Chain | Residue |
A | LYS3 |
A | LYS30 |
A | TYR31 |
A | CYS41 |
A | GLU43 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 103 |
Chain | Residue |
A | ARG21 |
A | ASN24 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PT B 101 |
Chain | Residue |
B | LYS3 |
B | GLU5 |
B | CYS41 |
B | SO4104 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 102 |
Chain | Residue |
B | GLU5 |
B | LEU65 |
B | GLY66 |
B | LEU67 |
B | GLU68 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 103 |
Chain | Residue |
B | GLY27 |
B | GLY28 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 104 |
Chain | Residue |
B | LYS3 |
B | ASP32 |
B | CYS41 |
B | PT101 |
B | HOH215 |
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 | 4 |
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 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER47 | |
B | SER47 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O08997 |
Chain | Residue | Details |
A | LYS60 | |
B | LYS60 |