V5YM14: Dipeptidyl aminopeptidase BII (dapb2)

Dipeptidyl aminopeptidase BII (dapb2) is a 722-residue protein from Pseudoxanthomonas mexicana. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: V5YM14.

Gene
dapb2
Organism
Pseudoxanthomonas mexicana
Length
722 residues
Mean pLDDT
95.3
Model
AF-V5YM14-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 95.3 (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 accurate92%
70 to 90Confident: backbone generally right4%
50 to 70Low: treat with caution0%
Below 50Very low: often disordered regions3%

What pLDDT means and how to read it

Function

Exopeptidase that catalyzes the removal of dipeptide units (NH2-P2-P1-) from the free amino termini of oligopeptides and small proteins (PubMed:24598890, PubMed:24827749, PubMed:8892831). Peptide digestion is sequential and substrate recognition is non-specific, with the exception that Pro is not suitable as a P1 residue (PubMed:24827749). Removes many residues of bioactive oligopeptides such as angiotensin I and neuromedin N and also cleaves oxidized insulin B chain. Able to hydrolyze an X-Pro bond, an imido bond. No endopeptidase activity (PubMed:8892831). May play a physiological role in feeding (PubMed:24598890)

Subunit structure

Homodimer

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3WOLX-ray1.74 ÅA/B=25-722
3WONX-ray1.75 ÅA/B=25-722
3WOOX-ray1.8 ÅA/B=25-722
3WOQX-ray1.82 ÅA/B=25-722
3WOMX-ray1.86 ÅA/B=25-722
3WOKX-ray1.95 ÅA/B=25-722
3WOPX-ray1.95 ÅA/B=25-722
3WOIX-ray2.1 ÅA/B=25-722
3WORX-ray2.1 ÅA/B=25-722
4Y06X-ray2.18 ÅA/B=1-722
3WOJX-ray2.2 ÅA/B=25-722

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