8KDX: Tyrosine-protein kinase Fyn

Tau-S214 Phosphorylation Inhibits Fyn Kinase Interaction and Increases the Decay Time of NMDAR-mediated Current. Determined by X-ray diffraction at 1.01 Å resolution. Released 28 Feb 2024.

Method
X-ray diffraction
Resolution
1.01 Å
Organism
Homo sapiens
Chains
2
Atoms
724
Mol. weight
8.5 kDa
Released
28 Feb 2024

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

Secondary structure: helices and β-sheets

8KDX contains 3 α-helices and 8 β-strands across 2 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: 2 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand87-8931
β-strand9312
β-strand10011
α-helix101-1022
β-strand10312
β-strand108-11361
β-strand119-12461
β-strand130-13451
α-helix135-1373
β-strand138-14031
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix216-2183

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tyrosine-protein kinase FynAprotein61Homo sapiensP06241 (AlphaFold model)
Microtubule-associated protein tauBprotein15Homo sapiensP10636 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8KDX_1 Tyrosine-protein kinase Fyn (chains A)
SGTTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPV
D
Sequence of entity 2 (B), FASTA
>8KDX_2 Microtubule-associated protein tau (chains B)
GSRSRTPSLPTPPTR

Primary citation

Tau-S214 Phosphorylation Inhibits Fyn Kinase Interaction and Increases the Decay Time of NMDAR-mediated Current. Jos, S., Poulose, R., Kambaru, A. et al. J Mol Biol (2024) 436:168445-168445. DOI 10.1016/j.jmb.2024.168445 · PubMed

Other PDB entries of the same protein (UniProt P06241 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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