P14904: Vacuolar aminopeptidase 1 (APE1)

Vacuolar aminopeptidase 1 (APE1) is a 514-residue protein from Saccharomyces cerevisiae (strain ATCC 204508 / S288c). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P14904.

Gene
APE1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
514 residues
Mean pLDDT
94.0
Model
AF-P14904-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 94.0 (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 accurate89%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions5%

What pLDDT means and how to read it

Function

Resident vacuolar enzyme that catalyzes the removal of amino acids from the N-terminus of peptides and proteins. Also acts as the major cargo protein of the cytoplasm-to-vacuole targeting (Cvt) pathway. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and the propeptide mediates the aggregation of dodecamers into higher multimers. The multimers are then recognized via the propeptide by their receptor ATG19, and ATG19 further interacts with ATG11, which tethers the APE1-ATG19 complex to the pre-autophagosomal structure (PAS). The cargo-receptor complex (also Cvt complex) is selectively enwrapped by a double-membrane structure termed the Cvt vesicle under vegetative…

Subunit structure

Homododecamer. The precursor form of aminopeptidase 1 (prApe1) assembles into dodecamers and further aggregates into higher multimers (the Ape1 complex) in the cytoplasm. The Ape1 complex is disaggregated in the vacuolar lumen, but mature aminopeptidase 1 (mApe1) retains its dodecameric form. Dodecamer assembly in the cytoplasm is essential for formation of an enzymatically active complex. If…

Subcellular location

Vacuole

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5JGFX-ray1.83 ÅA/B/C/D=46-514
5JGEX-ray1.91 ÅC/F=1-20
5JH9X-ray2.1 ÅA/B/C/D=1-514
4R8FX-ray2.5 ÅA/B/C/D=46-514
5JHCX-ray3.4 ÅA/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-22
5JM9EM24.0 ÅA=1-514

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