Q15389: Angiopoietin-1 (ANGPT1)

Angiopoietin-1 (ANGPT1) is a 498-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15389.

Gene
ANGPT1
Organism
Homo sapiens
Length
498 residues
Mean pLDDT
83.1
Model
AF-Q15389-F1 v6
Model created
1 Aug 2025
PDB structures
5

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Model confidence (pLDDT)

The mean pLDDT of this model is 83.1 (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 accurate67%
70 to 90Confident: backbone generally right14%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions15%

What pLDDT means and how to read it

Function

Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK…

Subunit structure

Homooligomer (PubMed:28601681). Interacts with TEK/TIE2 (PubMed:28601681, PubMed:30689269). 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 (PubMed:29323190)

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
9IVTX-ray1.75 ÅA=283-498
4EPUX-ray2.1 ÅA/B=282-497
9IVUX-ray2.28 ÅA=283-498
4JYOX-ray2.5 ÅX=280-498
4K0VX-ray4.51 ÅB=280-498

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