6YJD: Capsid assembly scaffolding protein,Prelamin-A/C

Lamin A coil2 dimer stabilized by N-terminal capping. Determined by X-ray diffraction at 2.9 Å resolution. Released 24 Feb 2021.

Method
X-ray diffraction
Resolution
2.9 Å
Organisms
Bacillus phage phi29, Homo sapiens
Chains
1
Atoms
844
Mol. weight
15.29 kDa
Ligands
NI
Released
24 Feb 2021

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

Secondary structure: helices and β-sheets

6YJD contains 3 α-helices and 0 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: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix279-2813
α-helix282-29312
α-helix299-37981

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Capsid assembly scaffolding protein,Prelamin-A/CAprotein127Bacillus phage phi29, Homo sapiensP02545 (AlphaFold model), P13848
Sequence of entity 1 (A), FASTA
>6YJD_1 Capsid assembly scaffolding protein,Prelamin-A/C (chains A)
GMPLKPEEHEDILNKLLDPELAQSERTEALQQLRVNYGSCVSEYNDLTKSLARERDTSRR
LLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQ
RSRGRAS

Ligands and cofactors

IDNameFormulaCopies
NINickel (II) ionNi2

Water and common crystallization additives (CL, TRS) are not listed.

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:

Browse structure collections

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