P53611: Geranylgeranyl transferase type-2 subunit beta (RABGGTB)

Geranylgeranyl transferase type-2 subunit beta (RABGGTB) is a 331-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P53611.

Gene
RABGGTB
Organism
Homo sapiens
Length
331 residues
Mean pLDDT
96.7
Model
AF-P53611-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 96.7 (very high 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 accurate94%
70 to 90Confident: backbone generally right5%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A (PubMed:7991565). Catalytic subunit of the geranylgeranyl transferase type 3 (GGTase-3) complex (PubMed:31209342, PubMed:32128853). The GGTase-3 complex geranylgeranylates and targets FBXL2 to the cellular membranes, where FBXL2 forms part of the E3 ubiquitin-protein ligase complex SCF(FBXL2) that mediates the degradation of membrane-anchored proteins (PubMed:31209342, PubMed:32128853). The GGTase-3 complex geranylgeranylates Golgi v-SNARE protein YKT6 at 'Cys-194' and this prenylation…

Subunit structure

Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM (component A) mediates peptide substrate binding (PubMed:18532927). The Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to Rab protein binding; the association is stabilized by geranylgeranyl pyrophosphate (GGpp) (PubMed:18532927). The CHM:RGGT:Rab…

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
6O60X-ray2.5 ÅB=1-331
6J7XX-ray2.75 ÅB=1-331
6J7FX-ray2.88 ÅB=1-331
6J6XX-ray2.96 ÅB=1-331
6J74X-ray3.21 ÅB=1-331

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