Q16665: Hypoxia-inducible factor 1-alpha (HIF1A)

Hypoxia-inducible factor 1-alpha (HIF1A) is a 826-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q16665.

Gene
HIF1A
Organism
Homo sapiens
Length
826 residues
Mean pLDDT
60.8
Model
AF-Q16665-F1 v6
Model created
1 Aug 2025
PDB structures
25

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Model confidence (pLDDT)

The mean pLDDT of this model is 60.8 (low 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 accurate31%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions48%

What pLDDT means and how to read it

Function

Functions as a master transcriptional regulator of the adaptive response to hypoxia (PubMed:11292861, PubMed:11566883, PubMed:15465032, PubMed:16973622, PubMed:17610843, PubMed:18658046, PubMed:20624928, PubMed:22009797, PubMed:30125331, PubMed:9887100). Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia (PubMed:11292861, PubMed:11566883, PubMed:15465032, PubMed:16973622, PubMed:17610843, PubMed:20624928, PubMed:22009797, PubMed:30125331,…

Subunit structure

Interacts with the ARNT; forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:10944113, PubMed:20699359). Interacts with COPS5; the interaction increases the transcriptional activity of HIF1A through increased stability (By similarity). Interacts with EP300 (via TAZ-type 1 domains); the interaction is stimulated…

Subcellular location

Cytoplasm, Nucleus, Nucleus speckle

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4H6JX-ray1.52 ÅA=238-348
4AJYX-ray1.73 ÅH=559-577
6GMRX-ray1.75 ÅH=560-577
8HE0X-ray1.8 ÅB=717-757
5L9VX-ray1.83 ÅC/D=395-413
6GFXX-ray1.83 ÅD=560-577
1LM8X-ray1.85 ÅH=556-575
8HE3X-ray1.9 ÅB=749-757
5L9BX-ray1.95 ÅC/D=556-574
1LQBX-ray2.0 ÅD=549-582
3HQRX-ray2.0 ÅS=558-574
7QGSX-ray2.0 ÅB=794-826
7LVSX-ray2.02 ÅF=796-826
5JWPX-ray2.1 ÅB=788-806
5LASX-ray2.1 ÅC/D=395-413
1H2KX-ray2.15 ÅS=786-826
1H2LX-ray2.25 ÅS=786-826
6YW3X-ray2.28 ÅS=556-574
2ILMX-ray2.3 ÅS=786-826
3HQUX-ray2.3 ÅS=558-574

Showing 20 of 25 experimental structures (best resolution first).

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