5JV3: PDB entry 5JV3

The neck-linker and alpha 7 helix of Homo sapiens Eg5 fused to EB1. Determined by X-ray diffraction at 2.01 Å resolution. Released 3 Aug 2016.

Method
X-ray diffraction
Resolution
2.01 Å
Organism
Homo sapiens
Chains
4
Atoms
2,477
Mol. weight
35.86 kDa
Ligands
CA
Released
3 Aug 2016

Explore 5JV3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5JV3 contains 12 α-helices and 2 β-strands across 4 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, 0 β-strands

ElementResiduesLengthSheet
α-helix9-4941
α-helix56-6510
Chain B: 3 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix9-4941
α-helix51-533
α-helix56-6510
β-strand6711
β-strand7311
Chain C: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-63
α-helix8-4942
α-helix56-6510
Chain D: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix4-74
α-helix8-4942
α-helix51-533
α-helix56-6510

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Chimera protein of Kinesin-like protein KIF11 and Microtubule-associated protein RP/EB family…A, B, C, Dprotein76Homo sapiensP52732 (AlphaFold model), Q15691 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>5JV3_1 Chimera protein of Kinesin-like protein KIF11 and Microtubule-associated protein RP/EB family member 1 (chains A, B, C, D)
LSNQKLTKKALIKEYTEEIERLKRDLAALEKERDFYFGKLRNIELICQENEGENDPVLQR
IVDILYATDEGFVIPD

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa1

Primary citation

Family-specific Kinesin Structures Reveal Neck-linker Length Based on Initiation of the Coiled-coil. Phillips, R.K., Peter, L.G., Gilbert, S.P. et al. J Biol Chem (2016) 291:20372-20386. DOI 10.1074/jbc.M116.737577 · PubMed

Other PDB entries of the same protein (UniProt P52732 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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