6YSH: PDB entry 6YSH

Lamin A 1-70 coil1A dimer stabilized by C-terminal capping. Determined by X-ray diffraction at 2.83 Å resolution. Released 2 Sept 2020.

Method
X-ray diffraction
Resolution
2.83 Å
Organism
Homo sapiens
Chains
2
Atoms
1,382
Mol. weight
19.39 kDa
Released
2 Sept 2020

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

Secondary structure: helices and β-sheets

6YSH contains 6 α-helices and 0 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.

Chains A and B: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix30-8657
α-helix88-903
α-helix93-10210

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Prelamin-A/C,Microtubule-associated protein RP/EB family member 1Aprotein83Homo sapiensP02545 (AlphaFold model), Q15691 (AlphaFold model)
Prelamin-A/C,Microtubule-associated protein RP/EB family member 1Bprotein81Homo sapiensP02545 (AlphaFold model), Q15691 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6YSH_1 Prelamin-A/C,Microtubule-associated protein RP/EB family member 1 (chains A)
RITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVDFYFGKLRNIELIC
QENEGENDPVLQRIVDILYATDE
Sequence of entity 2 (B), FASTA
>6YSH_2 Prelamin-A/C,Microtubule-associated protein RP/EB family member 1 (chains B)
ITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVDFYFGKLRNIELICQ
ENEGENDPVLQRIVDILYATD

Primary citation

Addressing the Molecular Mechanism of Longitudinal Lamin Assembly Using Chimeric Fusions. Stalmans, G., Lilina, A.V., Vermeire, P.J. et al. Cells (2020) 9. DOI 10.3390/cells9071633 · PubMed

Other PDB entries of the same protein (UniProt P02545 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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