4MVI
Crystal structure of an engineered lipocalin (Anticalin US7) in complex with the Alzheimer amyloid peptide Abeta(1-40)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005506 | molecular_function | iron ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0006826 | biological_process | iron ion transport |
A | 0006915 | biological_process | apoptotic process |
A | 0015891 | biological_process | siderophore transport |
A | 0031410 | cellular_component | cytoplasmic vesicle |
A | 0035580 | cellular_component | specific granule lumen |
A | 0036094 | molecular_function | small molecule binding |
A | 0042742 | biological_process | defense response to bacterium |
A | 0042802 | molecular_function | identical protein binding |
A | 0045087 | biological_process | innate immune response |
A | 0060205 | cellular_component | cytoplasmic vesicle lumen |
A | 0070062 | cellular_component | extracellular exosome |
A | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
A | 0140315 | molecular_function | iron ion sequestering activity |
A | 1903981 | molecular_function | enterobactin binding |
B | 0016020 | cellular_component | membrane |
Functional Information from PROSITE/UniProt
site_id | PS00213 |
Number of Residues | 14 |
Details | LIPOCALIN Lipocalin signature. NFQdnQFHGKWYVV |
Chain | Residue | Details |
A | ASN21-VAL34 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11274207, ECO:0000269|PubMed:26898943 |
Chain | Residue | Details |
B | HIS6 | |
B | HIS14 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10413512, ECO:0000305|PubMed:11274207 |
Chain | Residue | Details |
B | TYR10 | |
A | ASN134 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10413512, ECO:0000269|PubMed:11274207, ECO:0000269|PubMed:26898943 |
Chain | Residue | Details |
B | HIS13 | |
A | TYR138 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Cleavage; by caspase-6; when associated with variant 670-N-L-671 |
Chain | Residue | Details |
B | ASP1 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Cleavage; by ACE => ECO:0000269|PubMed:11604391, ECO:0000269|PubMed:16154999 |
Chain | Residue | Details |
B | ASP7 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Cleavage; by alpha-secretase => ECO:0000305|PubMed:11851430 |
Chain | Residue | Details |
B | LYS16 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | SITE: Cleavage; by theta-secretase => ECO:0000269|PubMed:16816112 |
Chain | Residue | Details |
B | PHE19 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | SITE: Implicated in free radical propagation => ECO:0000250 |
Chain | Residue | Details |
B | GLY33 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | SITE: Susceptible to oxidation => ECO:0000269|PubMed:10535332 |
Chain | Residue | Details |
B | MET35 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | SITE: Cleavage; by gamma-secretase; site 1 => ECO:0000305|PubMed:11851430 |
Chain | Residue | Details |
B | VAL40 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (HexNAc...) tyrosine; partial => ECO:0000269|PubMed:22576872 |
Chain | Residue | Details |
B | TYR10 |