Q9DBG3: AP-2 complex subunit beta (Ap2b1)

AP-2 complex subunit beta (Ap2b1) is a 937-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q9DBG3.

Gene
Ap2b1
Organism
Mus musculus
Length
937 residues
Mean pLDDT
82.0
Model
AF-Q9DBG3-F1 v6
Model created
1 Aug 2025
PDB structures
9

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Model confidence (pLDDT)

The mean pLDDT of this model is 82.0 (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 accurate58%
70 to 90Confident: backbone generally right26%
50 to 70Low: treat with caution3%
Below 50Very low: often disordered regions13%

What pLDDT means and how to read it

Function

Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly…

Subunit structure

Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1) (By similarity). Interacts with EPN1 (By similarity). Interacts with EPS15; clathrin competes with EPS15 (By similarity). Interacts with SNAP91; clathrin…

Subcellular location

Cell membrane, Membrane, coated pit

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
9PWAEM2.55 ÅB=1-591
6OWOEM3.2 ÅB=1-591
8T1OEM3.3 ÅB=1-591
6OXLEM3.5 ÅB=1-591
7RW8EM3.5 ÅB=1-591
7RWCEM3.8 ÅB=1-591
7RW9EM3.9 ÅB=1-591
7RWBEM3.9 ÅB/b=1-591
7RWAEM4.7 ÅB/b=1-591

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