O15123: Angiopoietin-2 (ANGPT2)

Angiopoietin-2 (ANGPT2) is a 496-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O15123.

Gene
ANGPT2
Organism
Homo sapiens
Length
496 residues
Mean pLDDT
83.9
Model
AF-O15123-F1 v6
Model created
1 Aug 2025
PDB structures
6

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Model confidence (pLDDT)

The mean pLDDT of this model is 83.9 (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 accurate65%
70 to 90Confident: backbone generally right15%
50 to 70Low: treat with caution5%
Below 50Very low: often disordered regions15%

What pLDDT means and how to read it

Function

Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1 (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). Involved in the…

Subunit structure

Interacts with TEK/TIE2, competing for the same binding site as ANGPT1 (PubMed:12427764, PubMed:15284220, PubMed:19223473, PubMed:32908006, PubMed:9204896). Interacts with ITGA5 (PubMed:32908006). Interacts with SVEP1/polydom (By similarity). Interacts with THBD; this interaction significantly inhibits the generation of activated PC and TAFIa/CPB2 by the thrombin/thrombomodulin complex…

Subcellular location

Secreted

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4JZCX-ray1.9 ÅA=279-496
1Z3UX-ray2.25 ÅA/B/C/D=281-496
4ZFGX-ray2.27 ÅA=277-496
1Z3SX-ray2.35 ÅA/B=281-496
8VGPEM2.7 ÅA=277-496
2GY7X-ray3.7 ÅA=281-495

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