Vascular endothelial growth factor receptor 2 (KDR) is a 1356-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P35968.
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The mean pLDDT of this model is 71.1 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 24% |
| 70 to 90 | Confident: backbone generally right | 43% |
| 50 to 70 | Low: treat with caution | 8% |
| Below 50 | Very low: often disordered regions | 26% |
What pLDDT means and how to read it
Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates…
Homodimer in the presence of bound dimeric VEGFA, VEGFC or VEGFD ligands; monomeric in the absence of bound ligands. Can also form heterodimers with FLT1/VEGFR1 and KDR/VEGFR2. Interacts (tyrosine phosphorylated) with LFYN, NCK1, PLCG1. Interacts (tyrosine-phosphorylated active form preferentially) with DAB2IP (via C2 domain and active form preferentially); the interaction occurs at the late…
Cell junction, Endoplasmic reticulum, Cell membrane, Cytoplasm, Nucleus, Cytoplasmic vesicle, Early endosome, Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2XIR | X-ray | 1.5 Å | A=806-1171 |
| 3VO3 | X-ray | 1.52 Å | A=806-1171 |
| 6GQQ | X-ray | 1.52 Å | A=806-939, A=991-1171 |
| 3VHE | X-ray | 1.55 Å | A=811-1169 |
| 3WZD | X-ray | 1.57 Å | A=814-1172 |
| 3EWH | X-ray | 1.6 Å | A=815-1171 |
| 3VNT | X-ray | 1.64 Å | A=806-1171 |
| 1YWN | X-ray | 1.71 Å | A=806-1171 |
| 3BE2 | X-ray | 1.75 Å | A=815-1171 |
| 6XVJ | X-ray | 1.78 Å | A=806-1171 |
| 4ASE | X-ray | 1.83 Å | A=787-1171 |
| 6GQO | X-ray | 1.87 Å | A=806-939, A=991-1171 |
| 3WZE | X-ray | 1.9 Å | A=814-1172 |
| 2P2H | X-ray | 1.95 Å | A=815-1172 |
| 4AG8 | X-ray | 1.95 Å | A=806-1171 |
| 6XVK | X-ray | 1.99 Å | A=806-1171 |
| 4AGC | X-ray | 2.0 Å | A=787-1171 |
| 4ASD | X-ray | 2.03 Å | A=787-1171 |
| 2OH4 | X-ray | 2.05 Å | A=806-1171 |
| 6GQP | X-ray | 2.09 Å | A=806-1171 |
Showing 20 of 54 experimental structures (best resolution first).
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