Crystal structure of human apolipoprotein a-I. Determined by X-ray diffraction at 4.0 Å resolution. Released 4 Feb 1998.
Explore 1AV1 in 3D Show helices and sheets RCSB PDB PDBe
1AV1 contains 40 α-helices and 0 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 49-53 | 5 | |
| α-helix | 54-58 | 5 | |
| α-helix | 59-62 | 4 | |
| α-helix | 66-70 | 5 | |
| α-helix | 72-140 | 69 | |
| α-helix | 143-144 | 2 | |
| α-helix | 145-149 | 5 | |
| α-helix | 150-210 | 61 | |
| α-helix | 213-217 | 5 | |
| α-helix | 229-242 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 45-48 | 4 | |
| α-helix | 49-54 | 6 | |
| α-helix | 57-63 | 7 | |
| α-helix | 66 | 1 | |
| α-helix | 67-72 | 6 | |
| α-helix | 73-117 | 45 | |
| α-helix | 120-141 | 22 | |
| α-helix | 144-201 | 58 | |
| α-helix | 208-218 | 11 | |
| α-helix | 228-239 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apolipoprotein a-I | A, B, C, D | protein | 201 | Homo sapiens | P02647 (AlphaFold model) |
>1AV1_1 APOLIPOPROTEIN A-I (chains A, B, C, D) MLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLD DFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTH LAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVL ESFKVSFLSALEEYTKKLNTQ
Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Borhani, D.W., Rogers, D.P., Engler, J.A. et al. Proc Natl Acad Sci U S A (1997) 94:12291-12296. DOI 10.1073/pnas.94.23.12291 · PubMed
Other PDB entries of the same protein (UniProt P02647 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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