Pro-adrenomedullin (ADM) is a 185-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P35318.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 61.8 (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 band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 1% |
| 70 to 90 | Confident: backbone generally right | 26% |
| 50 to 70 | Low: treat with caution | 55% |
| Below 50 | Very low: often disordered regions | 19% |
What pLDDT means and how to read it
Adrenomedullin/ADM and proadrenomedullin N-20 terminal peptide/PAMP are peptide hormones that act as potent hypotensive and vasodilatator agents (PubMed:8387282, PubMed:9620797). Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, ADM is diuretic and natriuretic, and both ADM and PAMP inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels
Secreted
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 4RWF | X-ray | 1.76 Å | B=119-146 |
| 6V2E | X-ray | 1.83 Å | B=131-146 |
| 6UUS | EM | 2.4 Å | P=95-146 |
| 5V6Y | X-ray | 2.8 Å | E/F/G/H=131-146 |
| 6UUN | EM | 3.0 Å | P=95-146 |
| 7VV0 | EM | 3.5 Å | L=30-41 |
| 2FLY | NMR | A=22-41 | |
| 2L7S | NMR | A=95-146 |
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.