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4MVI

Crystal structure of an engineered lipocalin (Anticalin US7) in complex with the Alzheimer amyloid peptide Abeta(1-40)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006826biological_processiron ion transport
A0006915biological_processapoptotic process
A0015891biological_processsiderophore transport
A0031410cellular_componentcytoplasmic vesicle
A0035580cellular_componentspecific granule lumen
A0036094molecular_functionsmall molecule binding
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0045087biological_processinnate immune response
A0060205cellular_componentcytoplasmic vesicle lumen
A0070062cellular_componentextracellular exosome
A0120162biological_processpositive regulation of cold-induced thermogenesis
A0140315molecular_functioniron ion sequestering activity
A1903981molecular_functionenterobactin binding
B0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. NFQdnQFHGKWYVV
ChainResidueDetails
AASN21-VAL34

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:11274207, ECO:0000269|PubMed:26898943
ChainResidueDetails
BHIS6
BHIS14

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:10413512, ECO:0000305|PubMed:11274207
ChainResidueDetails
BTYR10
AASN134

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10413512, ECO:0000269|PubMed:11274207, ECO:0000269|PubMed:26898943
ChainResidueDetails
BHIS13
ATYR138

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Cleavage; by caspase-6; when associated with variant 670-N-L-671
ChainResidueDetails
BASP1

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Cleavage; by ACE => ECO:0000269|PubMed:11604391, ECO:0000269|PubMed:16154999
ChainResidueDetails
BASP7

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Cleavage; by alpha-secretase => ECO:0000305|PubMed:11851430
ChainResidueDetails
BLYS16

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Cleavage; by theta-secretase => ECO:0000269|PubMed:16816112
ChainResidueDetails
BPHE19

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Implicated in free radical propagation => ECO:0000250
ChainResidueDetails
BGLY33

site_idSWS_FT_FI9
Number of Residues1
DetailsSITE: Susceptible to oxidation => ECO:0000269|PubMed:10535332
ChainResidueDetails
BMET35

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Cleavage; by gamma-secretase; site 1 => ECO:0000305|PubMed:11851430
ChainResidueDetails
BVAL40

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: O-linked (HexNAc...) tyrosine; partial => ECO:0000269|PubMed:22576872
ChainResidueDetails
BTYR10

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PDB entries from 2024-07-31

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