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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
A0002020molecular_functionprotease binding
A0002376biological_processimmune system process
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006811biological_processmonoatomic ion transport
A0006826biological_processiron ion transport
A0006915biological_processapoptotic process
A0006953biological_processacute-phase response
A0006979biological_processresponse to oxidative stress
A0007614biological_processshort-term memory
A0007616biological_processlong-term memory
A0009410biological_processresponse to xenobiotic stimulus
A0009615biological_processresponse to virus
A0009617biological_processresponse to bacterium
A0009635biological_processresponse to herbicide
A0009636biological_processresponse to toxic substance
A0009637biological_processresponse to blue light
A0009750biological_processresponse to fructose
A0010040biological_processresponse to iron(II) ion
A0010046biological_processresponse to mycotoxin
A0010595biological_processpositive regulation of endothelial cell migration
A0010628biological_processpositive regulation of gene expression
A0015891biological_processsiderophore transport
A0031346biological_processpositive regulation of cell projection organization
A0031410cellular_componentcytoplasmic vesicle
A0031667biological_processresponse to nutrient levels
A0031669biological_processcellular response to nutrient levels
A0032496biological_processresponse to lipopolysaccharide
A0035580cellular_componentspecific granule lumen
A0036094molecular_functionsmall molecule binding
A0036295biological_processcellular response to increased oxygen levels
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0043065biological_processpositive regulation of apoptotic process
A0043525biological_processpositive regulation of neuron apoptotic process
A0045087biological_processinnate immune response
A0060205cellular_componentcytoplasmic vesicle lumen
A0070062cellular_componentextracellular exosome
A0070301biological_processcellular response to hydrogen peroxide
A0071222biological_processcellular response to lipopolysaccharide
A0071347biological_processcellular response to interleukin-1
A0071354biological_processcellular response to interleukin-6
A0071356biological_processcellular response to tumor necrosis factor
A0071456biological_processcellular response to hypoxia
A0071481biological_processcellular response to X-ray
A0097192biological_processextrinsic apoptotic signaling pathway in absence of ligand
A0110090biological_processpositive regulation of hippocampal neuron apoptotic process
A0110091biological_processnegative regulation of hippocampal neuron apoptotic process
A0120162biological_processpositive regulation of cold-induced thermogenesis
A0140315molecular_functioniron ion sequestering activity
A1903428biological_processpositive regulation of reactive oxygen species biosynthetic process
A1903981molecular_functionenterobactin binding
A1904373biological_processresponse to kainic acid
A1904440biological_processpositive regulation of iron ion import across plasma membrane
A1904646biological_processcellular response to amyloid-beta
A1905956biological_processpositive regulation of endothelial tube morphogenesis
A1990090biological_processcellular response to nerve growth factor stimulus
A2000379biological_processpositive regulation of reactive oxygen species metabolic process
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

237735

PDB entries from 2025-06-18

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