P62820: Ras-related protein Rab-1A (RAB1A)

Ras-related protein Rab-1A (RAB1A) is a 205-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62820.

Gene
RAB1A
Organism
Homo sapiens
Length
205 residues
Mean pLDDT
84.7
Model
AF-P62820-F1 v6
Model created
1 Aug 2025
PDB structures
15

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.7 (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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate68%
70 to 90Confident: backbone generally right13%
50 to 70Low: treat with caution7%
Below 50Very low: often disordered regions13%

What pLDDT means and how to read it

Function

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed:20639577, PubMed:20861236, PubMed:21303926, PubMed:22939626). 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 (PubMed:20639577, PubMed:20861236, PubMed:21303926, PubMed:22939626). RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone…

Subunit structure

May interact with YIPF5 (By similarity). Interacts with C9orf72; the interaction mediates recruitment of RAB1A to the ATG1/ULK1 kinase complex (PubMed:27334615). Interacts with GDI1; this promotes dissociation from membranes (PubMed:20176951, PubMed:23815289)

Subcellular location

Golgi apparatus, Endoplasmic reticulum, Early endosome, Cytoplasm, cytosol, Membrane, Melanosome

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
2WWXX-ray1.5 ÅA=4-178
7EQ2X-ray1.55 ÅA/B=1-176
3SFVX-ray1.73 ÅA=1-176
3TKLX-ray2.18 ÅA=1-191
2FOLX-ray2.63 ÅA=6-177
9MHFEM2.73 ÅE=1-205
4JVSX-ray2.78 ÅB=1-177
4FMCX-ray2.8 ÅB/D=6-176, F=14-115
3L0IX-ray2.85 ÅB/D=1-177
4FMDX-ray3.05 ÅB/D=6-176, F=13-176
4FMBX-ray3.2 ÅB/D/F=6-176
4IRUX-ray3.2 ÅB/D/F=4-177
9MHGEM3.2 ÅE=1-205
4FMEX-ray4.1 ÅB/E=6-176
9MHHEM4.5 ÅE=1-205

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