Current Protein Identity:Q969X0
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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 |
|---|---|---|---|---|---|---|---|
| 6RIR Crystal structure of phosphorylated Rab8a in complex with the Rab-binding domain of RILPL2 Deposited 2019-04-25 | Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count |
Chain C
129–165(37 aa)
Chain D
129–165(37 aa)
|
Not recorded | GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 GOL GLYCEROL × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;pH 7;290 K;8% PEG 8K
100mM Na HEPES
|
Resolution 1.77 Å R-free 0.210 |
| 6SQ2 Structure of a phosphomimetic switch 2 variant of Rab8a in complex with the phospho-Rab binding domain of RILPL2 Deposited 2019-09-03 | Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count |
Chain D
129–165(37 aa)
Chain E
129–165(37 aa)
|
Not recorded | GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;100mM HEPES
10% PEG 4,000
10% 2-propanol
|
Resolution 1.68 Å R-free 0.202 |
| 7LWB Crystal Structure of phospho-Rab8a with the RH2 domain (117-165) of RILPL2 Deposited 2021-02-28 | Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count |
Chain D
117–165(49 aa)
Fragment:RH2 domain
|
Not recorded | GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION;pH 7.5;288 K;150mM DL-Malic acid,
20% PEG3350
|
Resolution 1.90 Å R-free 0.267 |