P62744: AP-2 complex subunit sigma (Ap2s1)

AP-2 complex subunit sigma (Ap2s1) is a 142-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62744.

Gene
Ap2s1
Organism
Rattus norvegicus
Length
142 residues
Mean pLDDT
97.0
Model
AF-P62744-F1 v6
Model created
1 Aug 2025
PDB structures
4

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Model confidence (pLDDT)

The mean pLDDT of this model is 97.0 (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 accurate97%
70 to 90Confident: backbone generally right3%
50 to 70Low: treat with caution0%
Below 50Very low: often disordered regions0%

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 CCDC32; the interaction is direct and mediates association of CCDC32 with adaptor protein complex 2 (AP-2)

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
4NEEX-ray2.88 ÅD/F/I/L=1-142
6OWOEM3.2 ÅS=1-142
6OXLEM3.5 ÅS=1-142
6OWTEM3.8 ÅS=1-142

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