Ras-related protein Rab-11A (RAB11A) is a 216-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62491.
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The mean pLDDT of this model is 87.2 (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 | 7% |
| Below 50 | Very low: often disordered regions | 8% |
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 set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:15601896, PubMed:15689490, PubMed:17462998, PubMed:19542231, PubMed:20026645, PubMed:20890297, PubMed:21282656, PubMed:26032412). RAB11A regulates endocytic recycling (PubMed:20026645). Forms a functional Rab11/RAB11FIP3/dynein complex that regulates the movement of peripheral sorting endosomes (SE) along…
Interacts (GTP-bound form) with RAB11FIPs (via their C-termini) including RAB11FIP1, RAB11FIP2, RAB11FIP3, RAB11FIP4 and RAB11FIP5 effectors (PubMed:11495908, PubMed:11786538, PubMed:12470645, PubMed:15173169, PubMed:15181150, PubMed:15280022, PubMed:15601896, PubMed:16148947, PubMed:16905101, PubMed:17030804, PubMed:17229837, PubMed:20026645, PubMed:25673879, PubMed:26032412, PubMed:26258637,…
Cell membrane, Endosome membrane, Recycling endosome membrane, Cleavage furrow, Cytoplasmic vesicle, phagosome membrane, Golgi apparatus membrane, Golgi apparatus, trans-Golgi network, Cytoplasmic vesicle membrane, Cell projection, cilium
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 1OIX | X-ray | 1.7 Å | A=1-173 |
| 2D7C | X-ray | 1.75 Å | A/B=7-173 |
| 2HV8 | X-ray | 1.86 Å | A/B/C=6-175 |
| 1OIV | X-ray | 1.98 Å | A/B=1-173 |
| 1YZK | X-ray | 2.0 Å | A=8-175 |
| 4C4P | X-ray | 2.0 Å | A=1-173 |
| 1OIW | X-ray | 2.05 Å | A=1-173 |
| 5JCZ | X-ray | 2.06 Å | A/D/I=1-177 |
| 6IY1 | X-ray | 2.11 Å | A/B/C/E=9-173, D=7-173, F=6-173 |
| 4LX0 | X-ray | 2.19 Å | A/C=1-177 |
| 5EZ5 | X-ray | 2.4 Å | A/B=8-175 |
| 2GZD | X-ray | 2.44 Å | A/B=2-173 |
| 2GZH | X-ray | 2.47 Å | A=2-173 |
| 4LWZ | X-ray | 2.55 Å | A/C=1-177 |
| 4UJ5 | X-ray | 2.6 Å | A/B=6-186 |
| 5C46 | X-ray | 2.65 Å | F=1-216 |
| 4D0L | X-ray | 2.94 Å | B/D/F=1-216 |
| 4UJ3 | X-ray | 3.0 Å | A/D/G/J/M/P/S/V=4-186 |
| 8VOF | X-ray | 3.0 Å | B=1-216 |
| 6DJL | X-ray | 3.1 Å | A/F/G/H=1-216 |
Showing 20 of 30 experimental structures (best resolution first).
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