6TPT: Receptor-type tyrosine-protein phosphatase F

Crystal structures of FNIII domain three and four of the human leucocyte common antigen-related protein, LAR. Determined by X-ray diffraction at 3.2 Å resolution. Released 13 May 2020.

Method
X-ray diffraction
Resolution
3.2 Å
Organism
Homo sapiens
Chains
1
Atoms
1,534
Mol. weight
21.9 kDa
Released
13 May 2020

Explore 6TPT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6TPT contains 8 α-helices and 16 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: 8 helices, 16 β-strands

ElementResiduesLengthSheet
α-helix513-5153
β-strand519-52241
β-strand528-53141
α-helix533-5353
β-strand540-549102
β-strand552-561102
β-strand566-56941
β-strand577-586102
β-strand589-59022
α-helix592-5965
β-strand597-60042
α-helix601-6033
α-helix609-6102
β-strand611-61773
β-strand622-62873
α-helix629-6313
α-helix632-6343
β-strand641-64884
β-strand657-66374
β-strand668-67253
β-strand679-68794
β-strand692-69544
α-helix696-6983
β-strand699-70244

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Receptor-type tyrosine-protein phosphatase FAprotein195Homo sapiensP10586 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6TPT_1 Receptor-type tyrosine-protein phosphatase F (chains A)
PAQPADFQAEVESDTRIQLSWLLPPQERIIMYELVYWAAEDEDQQHKVTFDPTSSYTLED
LKPDTLYRFQLAARSDMGVGVFTPTIEARTAQSTPSAPPQKVMCVSMGSTTVRVSWVPPP
ADSRNGVITQYSVAYEAVDGEDRGRHVVDGISREHSSWDLVGLEKWTEYRVWVRAHTDVG
PGPESSPVLVRTDED

Primary citation

Crystal and solution structures of fragments of the human leucocyte common antigen-related protein. Vilstrup, J., Simonsen, A., Birkefeldt, T. et al. Acta Crystallogr D Struct Biol (2020) 76:406-417. DOI 10.1107/S2059798320003885 · PubMed

Other PDB entries of the same protein (UniProt P10586 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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