Annexin A2 (ANXA2) is a 339-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P07355.
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The mean pLDDT of this model is 94.3 (very high 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 | 91% |
| 70 to 90 | Confident: backbone generally right | 3% |
| 50 to 70 | Low: treat with caution | 2% |
| Below 50 | Very low: often disordered regions | 4% |
What pLDDT means and how to read it
Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:22848640, PubMed:24808179). Binds to endosomes damaged by phagocytosis of particulate wear debris and participates in endosomal membrane stabilization, thereby limiting NLRP3 inflammasome activation (By similarity). Required for endothelial cell surface plasmin generation and may support fibrinolytic…
Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2/p36 (By similarity). Interacts with ATP1B1 (By similarity). Interacts with DYSF (By similarity). Interacts with COCH (PubMed:21886777). Interacts (via repeat Annexin 1) with PCSK9 (via the C-terminal domain); the interaction inhibits the degradation of LDLR (PubMed:18799458). Interacts with CEACAM1 (via the…
Secreted, extracellular space, extracellular matrix, basement membrane, Melanosome
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2HYV | X-ray | 1.42 Å | A=32-339 |
| 1W7B | X-ray | 1.52 Å | A=1-339 |
| 7QQM | X-ray | 1.6 Å | A=23-339 |
| 7PC5 | X-ray | 1.7 Å | A=22-339 |
| 7P73 | X-ray | 1.85 Å | A=23-339 |
| 2HYU | X-ray | 1.86 Å | A=32-339 |
| 7ZVN | X-ray | 1.87 Å | A=34-339 |
| 5LPX | X-ray | 1.9 Å | A=2-339 |
| 7P74 | X-ray | 1.9 Å | A=22-339 |
| 7PC3 | X-ray | 1.95 Å | A=29-339 |
| 7P70 | X-ray | 2.0 Å | A=22-339 |
| 7PCB | X-ray | 2.0 Å | A=29-339 |
| 2HYW | X-ray | 2.1 Å | A/B=32-339 |
| 5LPU | X-ray | 2.1 Å | A/B=2-339 |
| 7NMI | X-ray | 2.1 Å | B=29-339 |
| 7PC7 | X-ray | 2.1 Å | A/B=22-339 |
| 7EQ7 | X-ray | 2.11 Å | A=1-339 |
| 7P72 | X-ray | 2.15 Å | A=22-339 |
| 8AEL | X-ray | 2.2 Å | A=22-339 |
| 5N7D | X-ray | 2.3 Å | A/B=22-339 |
Showing 20 of 41 experimental structures (best resolution first).
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