P18484: AP-2 complex subunit alpha-2 (Ap2a2)

AP-2 complex subunit alpha-2 (Ap2a2) is a 938-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P18484.

Gene
Ap2a2
Organism
Rattus norvegicus
Length
938 residues
Mean pLDDT
84.9
Model
AF-P18484-F1 v6
Model created
1 Aug 2025
PDB structures
15

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.9 (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 accurate62%
70 to 90Confident: backbone generally right28%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions9%

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). Interacts with clathrin (By similarity). Binds EPN1, EPS15, AMPH, SNAP91 and BIN1 (By similarity). Interacts with HIP1 (By similarity). Interacts with DGKD (By…

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
6QH5X-ray2.56 ÅA=1-620
2VGLX-ray2.59 ÅA=1-620
4UQIX-ray2.79 ÅA=1-620
4NEEX-ray2.88 ÅA/B/G/J=1-395
7OHOX-ray2.88 ÅAAA=1-620
6URIX-ray3.0 ÅA=1-620
2XA7X-ray3.1 ÅA=1-620
7OG1X-ray3.25 ÅAAA=1-620
6QH7X-ray3.4 ÅA=1-620
6OWTEM3.8 ÅA=1-938
6YAEEM3.9 ÅA=1-620
7Z5CEM4.16 ÅA=1-620
6QH6X-ray5.0 ÅA=1-620
6YAFEM9.1 ÅA=1-622
6YAHEM10.2 ÅA=1-622

More AlphaFold highlights

About this viewer

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