Q99P58: Ras-related protein Rab-27B (Rab27b)

Ras-related protein Rab-27B (Rab27b) is a 218-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q99P58.

Gene
Rab27b
Organism
Mus musculus
Length
218 residues
Mean pLDDT
85.4
Model
AF-Q99P58-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

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 bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate63%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions12%

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. 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 (By similarity). RAB27B regulates homeostasis of late endocytic pathway, including endosomal positioning, maturation and secretion (By similarity). Plays a role in NTRK2/TRKB axonal anterograde transport by facilitating the association of NTRK2/TRKB with KLC1 (By similarity). May be involved in targeting uroplakins to…

Subunit structure

Interacts with SYTL2, SYTL4, MYRIP and MLPH. Interacts with RPH3A and RPH3A. Interacts (GDP-bound form preferentially) with DENND10 (By similarity)

Subcellular location

Membrane, Late endosome

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
2IEZX-ray2.8 ÅA/B/H/I=1-218
2IF0X-ray2.8 ÅA/B=1-198
2ZETX-ray3.0 ÅA/B=1-201
2IEYX-ray3.18 ÅA/B=1-193

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