Q02763: Angiopoietin-1 receptor (TEK)

Angiopoietin-1 receptor (TEK) is a 1124-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q02763.

Gene
TEK
Organism
Homo sapiens
Length
1124 residues
Mean pLDDT
83.9
Model
AF-Q02763-F1 v6
Model created
1 Aug 2025
PDB structures
17

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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 accurate50%
70 to 90Confident: backbone generally right35%
50 to 70Low: treat with caution8%
Below 50Very low: often disordered regions7%

What pLDDT means and how to read it

Function

Tyrosine-protein kinase that acts as a cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Has anti-inflammatory effects by preventing the leakage of pro-inflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post-natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where…

Subunit structure

Homodimer. Heterodimer with TIE1. Interacts with ANGPT1, ANGPT2 and ANGPT4 (PubMed:15284220, PubMed:32908006, PubMed:9204896). At cell-cell contacts in quiescent cells, forms a signaling complex composed of ANGPT1 plus TEK molecules from two adjoining cells. In the absence of endothelial cell-cell contacts, interaction with ANGPT1 mediates contacts with the extracellular matrix. Interacts with…

Subcellular location

Cell membrane, Cell junction, Cell junction, focal adhesion, Cytoplasm, cytoskeleton, Secreted

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
3BEAX-ray2.02 ÅA=917-935
6MWEX-ray2.05 ÅA/B=808-1124
7E72X-ray2.09 ÅE/F=541-735
1FVRX-ray2.2 ÅA/B=808-1124
2OO8X-ray2.2 ÅX=808-1124
3L8PX-ray2.4 ÅA=808-1124
2P4IX-ray2.5 ÅA/B=808-1124
4X3JX-ray2.5 ÅA=802-1122
5UTKX-ray2.5 ÅA/B=442-741
5MYBX-ray2.6 ÅA/B=443-742
9LV4EM2.67 ÅB=23-452
2OSCX-ray2.8 ÅA=808-1124
2GY5X-ray2.9 ÅA=23-445
5MYAX-ray2.9 ÅA/B=443-742
2WQBX-ray2.95 ÅA=802-1124
2GY7X-ray3.7 ÅB=23-445
4K0VX-ray4.51 ÅA=23-542

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