Current Protein Identity:Q6V1Q9
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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 |
|---|---|---|---|---|---|---|---|
| 5BPV Crystal Structure of Zaire ebolavirus VP35 RNA binding domain mutant I278A Deposited 2015-05-28 | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain A
217–340(124 aa)
Fragment:RNA binding domain, UNP residues 217-340
|
Mutation:I278A | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;295 K;0.2 M potassium sodium tartrate tetrahydrate, 20% PEG 3350
|
Resolution 1.95 Å R-free 0.218 |
| 5BPV Crystal Structure of Zaire ebolavirus VP35 RNA binding domain mutant I278A Deposited 2015-05-28 | Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count |
Chain B
217–340(124 aa)
Fragment:RNA binding domain, UNP residues 217-340
|
Mutation:I278A | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;295 K;0.2 M potassium sodium tartrate tetrahydrate, 20% PEG 3350
|
Resolution 1.95 Å R-free 0.218 |
| 7D35 Human LC8 bound to ebola virus VP35(67-76) Deposited 2020-09-18 | Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count |
Chain B
67–76(10 aa)
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;293 K;200mM ammonium citrate dibasic, 200mM ammonium citrate tribasic (pH 5.5), 30% (w/v) polyethylene glycol 3350
|
Resolution 2.40 Å R-free 0.292 |