P84091: AP-2 complex subunit mu (Ap2m1)

AP-2 complex subunit mu (Ap2m1) is a 435-residue protein from Mus musculus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P84091.

Gene
Ap2m1
Organism
Mus musculus
Length
435 residues
Mean pLDDT
89.4
Model
AF-P84091-F1 v6
Model created
1 Aug 2025
PDB structures
10

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Model confidence (pLDDT)

The mean pLDDT of this model is 89.4 (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 accurate72%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Component of the adaptor protein complex 2 (AP-2) (PubMed:14745134, PubMed:15473838). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways (PubMed:14745134, PubMed:15473838). Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation (PubMed:14745134, PubMed:15473838). 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 (PubMed:14745134, PubMed:15473838). The clathrin lattice serves as a mechanical…

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 ATP6V1H and MEGF10 (By similarity). Interacts with EGFR and TTGN1 (By similarity). Interacts with F2R (By similarity). Interacts…

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 ÅM=1-435
6OWOEM3.2 ÅM=1-435
8T1OEM3.3 ÅM=1-435
6OXLEM3.5 ÅM=1-435
7RW8EM3.5 ÅM=1-435
6OWTEM3.8 ÅM=1-141
7RWCEM3.8 ÅM=1-435
7RW9EM3.9 ÅM=1-435
7RWBEM3.9 ÅM/m=1-435
7RWAEM4.7 ÅM/m=1-435

More AlphaFold highlights

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