8FZV: PDB entry 8FZV

The von Willebrand factor A domain of human capillary morphogenesis gene II, flexibly fused to the 1TEL crystallization chaperone, Ala-Ala linker variant, expressed with SUMO tag. Determined by X-ray diffraction at 3.29 Å resolution. Released 19 Jul 2023.

Method
X-ray diffraction
Resolution
3.29 Å
Organism
Homo sapiens
Chains
3
Atoms
4,021
Mol. weight
89.16 kDa
Ligands
MG
Released
19 Jul 2023

Explore 8FZV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8FZV contains 31 α-helices and 12 β-strands across 3 chains. 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: 13 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix13-153
α-helix18-3114
α-helix39-413
α-helix46-494
α-helix54-607
α-helix66-8116
β-strand83-9081
α-helix96-983
α-helix99-11012
β-strand118-12581
β-strand129-13681
α-helix139-15012
α-helix160-17415
β-strand181-18771
α-helix195-20814
β-strand212-21761
α-helix223-2297
β-strand236-23721
α-helix243-2497
Chain B: 12 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix13-153
α-helix18-3114
α-helix46-494
α-helix54-607
α-helix65-7915
β-strand84-8852
α-helix94-974
α-helix99-11214
β-strand120-12232
β-strand133-13642
α-helix139-15113
α-helix160-17415
β-strand181-18772
α-helix195-20814
β-strand211-21772
α-helix223-2297
β-strand23712
α-helix245-2528
Chain C: 6 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix13-153
α-helix18-3114
α-helix39-424
α-helix46-516
α-helix54-607
α-helix65-7814

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transcription factor ETV6,Anthrax toxin receptor 2A, B, Cprotein257Homo sapiensP41212 (AlphaFold model), P58335 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>8FZV_1 Transcription factor ETV6,Anthrax toxin receptor 2 (chains A, B, C)
GSIALPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYR
SPHSGDELYELLQHILAQARAAFDLYFVLDKSGSVANNWIEIYNFVQQLAERFVSPEMRL
SFIVFSSQATIILPLTGDRGKISKGLEDLKRVSPVGETYIHEGLKLANEQIQKAGGLKTS
SIIIALTDGKLDGLVPSYAEKEAKISRSLGASVYAVGVLDFEQAQLERIADSKEQVFPVK
GGFQALKGIINSILAQS

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

Water and common crystallization additives (UNX) are not listed.

Primary citation

Increasing the bulk of the 1TEL-target linker and retaining the 10×His tag in a 1TEL-CMG2-vWa construct improves crystal order and diffraction limits. Gajjar, P.L., Pedroza Romo, M.J., Litchfield, C.M. et al. Acta Crystallogr D Struct Biol (2023) 79:925-943. DOI 10.1107/S2059798323007246 · PubMed

Other PDB entries of the same protein (UniProt P41212 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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