Ras-related protein Rab-8A (RAB8A) is a 207-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P61006.
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The mean pLDDT of this model is 85.4 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 69% |
| 70 to 90 | Confident: backbone generally right | 16% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 13% |
What pLDDT means and how to read it
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB8A is involved in polarized vesicular trafficking and neurotransmitter release. Together with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (PubMed:20890297).…
Interacts (GTP-bound form) with MICALL1; regulates RAB8A association with recycling endosomes (By similarity). Interacts with MICALL2; competes with RAB13 and is involved in E-cadherin endocytic recycling (By similarity). Interacts (GTP-bound form) with MICAL1, MICALCL, MICAL3, EHBP1 and EHBP1L1; at least in case of MICAL1, MICALCL, MICAL3 and EHBP1L1 two molecules of RAB8A can bind to one…
Cell membrane, Golgi apparatus, Endosome membrane, Recycling endosome membrane, Cell projection, cilium, Cytoplasmic vesicle, phagosome, Cytoplasmic vesicle, phagosome membrane, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole, Cytoplasm, cytoskeleton, cilium basal…
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4LHW | X-ray | 1.55 Å | A/B/C/D/E=6-176 |
| 6SQ2 | X-ray | 1.68 Å | A/B=1-181 |
| 6WHE | X-ray | 1.73 Å | A/B=1-181 |
| 6RIR | X-ray | 1.77 Å | A/B=1-181 |
| 9M0O | X-ray | 1.83 Å | D=1-176 |
| 7LWB | X-ray | 1.9 Å | A=1-181 |
| 6ZSI | X-ray | 1.91 Å | A/B=1-176 |
| 9IKQ | X-ray | 1.93 Å | A/B=1-181 |
| 4LHV | X-ray | 1.95 Å | A/B/C/D/E=6-176 |
| 3QBT | X-ray | 2.0 Å | A/C/E/G=6-176 |
| 6ZSJ | X-ray | 2.0 Å | A/B=1-176 |
| 6YX5 | X-ray | 2.14 Å | A=6-176 |
| 7BWT | X-ray | 2.3 Å | B=2-183 |
| 6STF | X-ray | 2.4 Å | A/B/C/D/E=6-176 |
| 3TNF | X-ray | 2.5 Å | A=6-176 |
| 6STG | X-ray | 2.5 Å | A/B=6-176 |
| 5SZI | X-ray | 2.85 Å | A=1-207 |
| 4LHX | X-ray | 3.05 Å | A/B=1-184 |
| 4LHY | X-ray | 3.1 Å | A/B=1-184 |
| 4LHZ | X-ray | 3.2 Å | A/B=1-184 |
Showing 20 of 21 experimental structures (best resolution first).
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