4MVK: Engineered lipocalin

Crystal structure of an engineered lipocalin (Anticalin US7) in complex with the Alzheimer amyloid peptide fragment VFFAED. Determined by X-ray diffraction at 1.5 Å resolution. Released 12 Aug 2015.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Homo sapiens
Chains
2
Atoms
1,598
Mol. weight
22.28 kDa
Released
12 Aug 2015

Explore 4MVK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4MVK contains 9 α-helices and 11 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 9 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix8-125
α-helix13-153
α-helix24-274
β-strand29-38101
α-helix47-493
β-strand5012
α-helix511
β-strand53-5861
β-strand64-7181
β-strand76-85101
β-strand91-9441
β-strand104-113101
β-strand118-127101
β-strand130-139101
α-helix146-15813
α-helix163-1653
β-strand166-16721
α-helix1691
β-strand17012
α-helix1711

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Neutrophil gelatinase-associated lipocalinAprotein188Homo sapiensP80188 (AlphaFold model)
Amyloid peptide fragment VFFAEDBprotein8Homo sapiensP05067 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4MVK_1 Neutrophil gelatinase-associated lipocalin (chains A)
QDSTSDLIPAPPLSKVPLQQNFQDNQFHGKWYVVGVAGNKSLREDKDPWKMYATIYELKE
DKSYNVTSVGFGTKKCHYKIRTFVPGSQPGEFTLGRIKSRPGRTSALVRVVSTNYNQHAM
VFFKVVQQNRESFNITLYGRTKELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDGSA
WSHPQFEK
Sequence of entity 2 (B), FASTA
>4MVK_2 Amyloid peptide fragment VFFAED (chains B)
XVFFAEDX

Primary citation

High-affinity Anticalins with aggregation-blocking activity directed against the Alzheimer beta-amyloid peptide. Rauth, S., Hinz, D., Borger, M. et al. Biochem J (2016) 473:1563-1578. DOI 10.1042/BCJ20160114 · PubMed

Other PDB entries of the same protein (UniProt P80188 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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