8YFK: FIP200 claw/TNIP1_FIR_pS123

Crystal structure of FIP200 claw/TNIP1_FIR_pS123. Determined by X-ray diffraction at 2.0 Å resolution. Released 14 Aug 2024.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
8
Atoms
3,516
Mol. weight
53.4 kDa
Ligands
MG
Released
14 Aug 2024

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

Secondary structure: helices and β-sheets

8YFK contains 11 α-helices and 34 β-strands across 8 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: 3 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand1495-149621
β-strand1506-151271
β-strand1517-152041
β-strand1528-153031
α-helix15311
α-helix1532-15343
α-helix1536-15383
β-strand1554-1567141
β-strand1581-158881
Chains B, D, F and H: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand106-10831
Chain C: 2 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand1495-149734
β-strand1506-151274
β-strand1517-152044
β-strand1528-153034
α-helix15311
α-helix1532-15343
β-strand1554-1567144
β-strand1581-158884
Chains E and G: 3 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand1496-149724
β-strand1506-151274
β-strand1517-152044
β-strand1528-153034
α-helix15311
α-helix1535-15373
β-strand154115
β-strand154514
α-helix1548-15514
β-strand155415
β-strand1555-1567134
β-strand1581-158994

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RB1-inducible coiled-coil protein 1A, C, E, Gprotein105Homo sapiensQ8TDY2 (AlphaFold model)
TNIP1_FIR_pS123 peptideB, D, F, Hprotein11Homo sapiensQ15025 (AlphaFold model)
Sequence of entity 1 (A, C, E, G), FASTA
>8YFK_1 RB1-inducible coiled-coil protein 1 (chains A, C, E, G)
SRHSEKIAIRDFQVGDLVLIILDERHDNYVLFTVSPTLYFLHSESLPALDLKPGEGASGA
SRRPWVLGKVMEKEYCQAKKAQNRFKVPLGTKFYRVKAVSWNKKV
Sequence of entity 2 (B, D, F, H), FASTA
>8YFK_2 TNIP1_FIR_pS123 peptide (chains B, D, F, H)
SSGTSSEFEVV

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2

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

Primary citation

Structural basis for TNIP1 binding to FIP200 during mitophagy. Wu, S., Li, M., Wang, L. et al. J Biol Chem (2024) 300:107605-107605. DOI 10.1016/j.jbc.2024.107605 · PubMed

Other PDB entries of the same protein (UniProt Q8TDY2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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