O00203: AP-3 complex subunit beta-1 (AP3B1)

AP-3 complex subunit beta-1 (AP3B1) is a 1094-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O00203.

Gene
AP3B1
Organism
Homo sapiens
Length
1094 residues
Mean pLDDT
75.3
Model
AF-O00203-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 75.3 (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 accurate49%
70 to 90Confident: backbone generally right24%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions25%

What pLDDT means and how to read it

Function

Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals

Subunit structure

Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or AP3S2) (Probable). AP-3 associates with the BLOC-1 complex (By similarity). Interacts with KIF3A; interaction is direct; interaction is impaired by…

Subcellular location

Cytoplasmic vesicle, clathrin-coated vesicle membrane, Golgi apparatus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9C5CEM3.6 ÅB=40-650
9C5AEM4.2 ÅB/b=1-677
9C59EM4.3 ÅB/b=1-677
9C5BEM4.5 ÅB=1-677
9C58EM4.7 ÅB=1-677

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