8FT6: PDB entry 8FT6

The von Willebrand factor A domain of human capillary morphogenesis gene II, flexibly fused to the 1TEL crystallization chaperone, Ala-Ala linker variant, SUMO tag-free preparation. Determined by X-ray diffraction at 2.62 Å resolution. Released 22 Mar 2023.

Method: X-ray diffraction
Resolution: 2.62 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,920
Mol. weight: 30.51 kDa
Ligands: CIT
Released: 22 Mar 2023

Explore 8FT6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8FT6 contains 14 α-helices and 6 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: 14 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	23-25	3
α-helix	28-41	14
α-helix	56-59	4
α-helix	64-70	7
α-helix	75-86	12
β-strand	93-100	8	1
α-helix	103-108	6
α-helix	109-122	14
β-strand	129-135	7	1
β-strand	139-146	8	1
α-helix	149-160	12
α-helix	170-183	14
β-strand	190-197	8	1
α-helix	205-218	14
β-strand	221-227	7	1
α-helix	233-239	7
α-helix	243-245	3
β-strand	246-248	3	1
α-helix	249-251	3
α-helix	253-266	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transcription factor ETV6,Anthrax toxin receptor 2 chimera	A	protein	266	Homo sapiens	P41212 (AlphaFold model), P58335 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8FT6_1 Transcription factor ETV6,Anthrax toxin receptor 2 chimera (chains A)
HHHHHHHHHHSIALPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLL
LTKEDFRYRSPHSGDELYELLQHILAQARAAFDLYFVLDKSGSVANNWIEIYNFVQQLAE
RFVSPEMRLSFIVFSSQATIILPLTGDRGKISKGLEDLKRVSPVGETYIHEGLKLANEQI
QKAGGLKTSSIIIALTDGKLDGLVPSYAEKEAKISRSLGASVYAVGVLDFEQAQLERIAD
SKEQVFPVKGGFQALKGIINSILAQS

Ligands and cofactors

ID	Name	Formula	Copies
CIT	Citric acid	C6 H8 O7	1

Water and common crystallization additives (IOD, SO4) 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:

9DOC 1.19 Å, The von Willebrand factor A domain of human capillary morphogenesis gene II, flexibly…
9ZB7 1.24 Å, A DARPin fused to the 1TEL crystallization chaperone via a direct helical fusion
9Q4D 1.3 Å, A DARPin fused to the double trigger 1TEL variant crystallization chaperone via a direct…
7TW9 1.41 Å, Structure of nsp14 N7-MethylTransferase domain fused with TELSAM bound to Sinefungin
1JI7 1.45 Å, Crystal Structure of TEL SAM Polymer
7TDY 1.53 Å, The ubiquitin-associated domain of human thirty-eight negative kinase 1, flexibly fused…
7TW8 1.55 Å, Structure of nsp14 N7-MethylTransferase domain fused with TELSAM bound to SAH
8FRJ 1.57 Å, Structure of nsp14 N7-MethylTransferase domain fused with TELSAM bound to SGC0946
9DB5 1.57 Å, A DARPin fused to the 1TEL crystallization chaperone via a proline-alanine linker
8FT8 1.6 Å, The von Willebrand factor A domain of human capillary morphogenesis gene II, flexibly…
8FRK 1.61 Å, Structure of nsp14 N7-MethylTransferase domain fused with TELSAM bound to SGC8158
7TW7 1.62 Å, Structure of nsp14 N7-MethylTransferase domain fused with TELSAM bound to SAM

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