Protein AMBP (AMBP) is a 352-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P02760.
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The mean pLDDT of this model is 81.5 (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 | 56% |
| 70 to 90 | Confident: backbone generally right | 22% |
| 50 to 70 | Low: treat with caution | 5% |
| Below 50 | Very low: often disordered regions | 17% |
What pLDDT means and how to read it
Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments (PubMed:11877257, PubMed:15683711, PubMed:22096585, PubMed:23157686, PubMed:23642167, PubMed:25698971, PubMed:32092412, PubMed:32823731). Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis (PubMed:11877257, PubMed:32092412). Reduces extracellular methemoglobin, a Fe3+ (ferric)…
Monomer (PubMed:22512701, PubMed:9183005). Homodimer (PubMed:9183005). In plasma, it occurs as a monomer or dimer and in covalently-linked complexes with immunoglobulin A (IgA), ALB/albumin and F2/prothrombin (PubMed:9183005). Chromophore-bound alpha-1-microglobulin interacts with the constant region of immunoglobulin A (PubMed:9183005). Chromophore-bound alpha-1-microglobulin interacts with ALB…
Secreted, Endoplasmic reticulum, Cytoplasm, cytosol, Cell membrane, Nucleus membrane, Mitochondrion inner membrane, Secreted, extracellular space, extracellular matrix
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6EJA | X-ray | 1.94 Å | B=210-221 |
| 4ES7 | X-ray | 2.0 Å | A=27-193 |
| 6EJ7 | X-ray | 2.0 Å | B=210-221 |
| 6EJ9 | X-ray | 2.02 Å | B=210-220 |
| 6EJC | X-ray | 2.06 Å | B=210-221 |
| 6EJ8 | X-ray | 2.09 Å | B=210-221 |
| 3QKG | X-ray | 2.3 Å | A=20-202 |
| 1BIK | X-ray | 2.5 Å | A=206-352 |
| 4U30 | X-ray | 2.5 Å | W/X/Y/Z=283-340 |
| 6EJB | X-ray | 2.56 Å | B=210-221 |
| 6EJD | X-ray | 2.68 Å | B=210-221 |
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