Current Protein Identity:Q7Z406 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
5I4E Crystal Structure of Human Nonmuscle Myosin 2C motor domain Deposited 2016-02-11 Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 47–784(738 aa) Fragment:UNP residues 265-489,UNP residues 265-489
Not recorded AOV ADP ORTHOVANADATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;281.15 K;TRIS PH 8.2, PEG 5K MME, MPD, NACL.
Resolution 2.25 Å R-free 0.241
5JLH Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution Deposited 2016-04-27 Assembly 1 Insufficient information Heteromer;Protein × 11 PDB declaration: undecameric(11) Consistent with protein count
Chain F 1–799(799 aa)
Chain G 1–799(799 aa)
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5;5 mM Tris-HCl pH 7.5, 1 mM DTT, 100 mM KCl, and 2 mM MgCl2
cryo-EM vitrification conditions Cryogen ETHANE;Sample (2 uL of F-actin-tropomyosin solution) was applied to a glow-discharged holey carbon grid, incubated for 20 s and manually blotted from the backside for less than a second with filter paper. Afterwards 1.5 uL of myosin solution (3 uM without nucleotide) were added directly on the grid, incubated for 10 s and then manually blotted for 5 s from the backside with filter paper.
Resolution 3.90 Å