Current Protein Identity:P03689 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
6BBM Mechanisms of Opening and Closing of the Bacterial Replicative Helicase: The DnaB Helicase and Lambda P Helicase Loader Complex Deposited 2017-10-18 Assembly 1 Protein heterocomplex Heteromer;Protein × 11 PDB declaration: undecameric(11) Consistent with protein count
Chain V 1–107(107 aa)
Chain W 1–107(107 aa)
Chain X 1–107(107 aa)
Chain Y 1–107(107 aa)
Chain Z 1–107(107 aa)
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5;Concentrated BP sample (18mg/mL) was diluted with freshly prepared buffer to desired concentration (~1.5 micromolar) for grid preparation.
cryo-EM vitrification conditions Cryogen ETHANE;3uL of sample was adhered to a fresh plasma cleaned grid and allowed to adsorb for 30 seconds, blotted for 3 seconds with a blot force of 4 and plunge frozen into liquid nitrogen-cooled ethane.
Resolution 4.10 Å
8V9S Distinct Quaternary States, Intermediates, and Autoinhibition During Loading of the DnaB-Replicative Helicase by the Phage Lambda P Helicase Loader Deposited 2023-12-09 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 105–210(106 aa) Fragment:residues 105 to 210
Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;298.15 K;Crystals were prepared using the sitting drop vapor diffusion method by mixing either 0.1, or 0.2, or 0.4 uL of the protein solution and 0.2 uL of a series of commercially available crystallization screens (Qiagen). Optimized crystals for X-ray diffraction were grown at room temperature in a buffer consisting of 3 M to 4 M NaCl with 0.1 M HEPES-NaOH, pH 7 to 8 and required 7 days to form.
Resolution 1.86 Å R-free 0.244
8V9T Ecoli DnaB helicase and Phage Lambda loader P with ADP-Mg in a 6:5 stoichiometry ratio Deposited 2023-12-09 Assembly 1 Protein heterocomplex Heteromer;Protein × 11 PDB declaration: undecameric(11) Consistent with protein count
Chain V 1–233(233 aa)
Chain W 1–233(233 aa)
Chain X 1–233(233 aa)
Chain Y 1–233(233 aa)
Chain Z 1–233(233 aa)
Mutation:K2E Mutation:K2E Mutation:K2E Mutation:K2E Mutation:K2E ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5;20 mM Na-HEPES pH 7.5, 450mM NaCl, 2mM DTT, 0.5mM MgCl2, 0.2mM ATP, 0.25% Glycerol
cryo-EM vitrification conditions Cryogen ETHANE;Protein BP (1.5 uM) and DNA (1.875 uM) was mixed in a 1.25 molar excess. 3uL of the sample was added to a plasma-cleaned grid at 4 degrees celsius, 100 percent humidity, blot force 4, blot time 4s, wait time 30s, total blots 1, and plunge-frozen into liquid nitrogen-cooled ethane.
Resolution 2.84 Å
9OA1 Ecoli DnaB helicase and Phage Lambda loader P with ADP-Mg in a 6:5 stoichiometry ratio. Deposited 2025-04-18 Assembly 1 Protein heterocomplex Heteromer;Protein × 11 PDB declaration: undecameric(11) Consistent with protein count
Chain V 1–233(233 aa)
Chain W 1–233(233 aa)
Chain X 1–233(233 aa)
Chain Y 1–233(233 aa)
Chain Z 1–233(233 aa)
Mutation:K2E Mutation:K2E Mutation:K2E Mutation:K2E Mutation:K2E ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5;20 mM Na-HEPES pH 7.5, 450mM NaCl, 2mM DTT, 0.5mM MgCl2, 0.2mM ATP, 0.25% Glycerol
cryo-EM vitrification conditions Cryogen ETHANE;Protein BP (1.5 uM) and DNA (1.875 uM) was mixed in a 1.25 molar excess. 3uL of the sample was added to a plasma-cleaned grid at 4 degrees celsius, 100 percent humidity, blot force 4, blot time 4s, wait time 30s, total blots 1, and plunge-frozen into liquid nitrogen-cooled ethane.
Resolution 2.66 Å
9OA2 Ecoli DnaB helicase and Phage Lambda loader P with ADP-Mg in a 6:6 stoichiometry ratio. Deposited 2025-04-18 Assembly 1 Protein heterocomplex Heteromer;Protein × 12 PDB declaration: dodecameric(12) Consistent with protein count
Chain U 1–233(233 aa)
Chain V 1–233(233 aa)
Chain W 1–233(233 aa)
Chain X 1–233(233 aa)
Chain Y 1–233(233 aa)
Chain Z 1–233(233 aa)
Mutation:K2E Mutation:K2E Mutation:K2E Mutation:K2E Mutation:K2E Mutation:K2E ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5;20 mM Na-HEPES pH 7.5, 450mM NaCl, 2mM DTT, 0.5mM MgCl2, 0.2mM ATP, 0.25% Glycerol
cryo-EM vitrification conditions Cryogen ETHANE;Protein BP (1.5 uM), ssDNA (1.875 uM), and LO-156-299-NHis (2.25 uM) was mixed at 1.25 and 1.5 molar excess, respectively. 3uL of the sample was added to a plasma-cleaned grid at 4 degrees celsius, 100 percent humidity, blot force 4, blot time 4s, wait time 30s, total blots 1, and plunge-frozen into liquid nitrogen-cooled ethane.
Resolution 3.85 Å