Crystal structure of human serum albumin. Determined by X-ray diffraction at 2.5 Å resolution. Released 27 May 1998.
Explore 1AO6 in 3D Show helices and sheets RCSB PDB PDBe
1AO6 contains 74 α-helices and 0 β-strands across 2 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 | 6-30 | 25 | |
| α-helix | 36-55 | 20 | |
| α-helix | 66-78 | 13 | |
| α-helix | 81-84 | 4 | |
| α-helix | 85-88 | 4 | |
| α-helix | 90-92 | 3 | |
| α-helix | 97-104 | 8 | |
| α-helix | 113-115 | 3 | |
| α-helix | 120-129 | 10 | |
| α-helix | 131-145 | 15 | |
| α-helix | 151-168 | 18 | |
| α-helix | 174-201 | 28 | |
| α-helix | 202-206 | 5 | |
| α-helix | 208-222 | 15 | |
| α-helix | 228-246 | 19 | |
| α-helix | 250-266 | 17 | |
| α-helix | 268-271 | 4 | |
| α-helix | 283-291 | 9 | |
| α-helix | 294-299 | 6 | |
| α-helix | 306 | 1 | |
| α-helix | 307-311 | 5 | |
| α-helix | 315-321 | 7 | |
| α-helix | 323-336 | 14 | |
| α-helix | 343-360 | 18 | |
| α-helix | 366-369 | 4 | |
| α-helix | 370-372 | 3 | |
| α-helix | 373-376 | 4 | |
| α-helix | 378-398 | 21 | |
| α-helix | 400-414 | 15 | |
| α-helix | 420-431 | 12 | |
| α-helix | 434-437 | 4 | |
| α-helix | 445-466 | 22 | |
| α-helix | 471-479 | 9 | |
| α-helix | 484-490 | 7 | |
| α-helix | 511-514 | 4 | |
| α-helix | 518-533 | 16 | |
| α-helix | 542-558 | 17 | |
| α-helix | 566-581 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-30 | 25 | |
| α-helix | 36-55 | 20 | |
| α-helix | 66-78 | 13 | |
| α-helix | 81-84 | 4 | |
| α-helix | 85-88 | 4 | |
| α-helix | 90-92 | 3 | |
| α-helix | 97-104 | 8 | |
| α-helix | 120-129 | 10 | |
| α-helix | 131-143 | 13 | |
| α-helix | 151-168 | 18 | |
| α-helix | 174-201 | 28 | |
| α-helix | 202-206 | 5 | |
| α-helix | 208-222 | 15 | |
| α-helix | 228-246 | 19 | |
| α-helix | 250-266 | 17 | |
| α-helix | 267-270 | 4 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-279 | 4 | |
| α-helix | 283-292 | 10 | |
| α-helix | 293-299 | 7 | |
| α-helix | 306-311 | 6 | |
| α-helix | 315-337 | 23 | |
| α-helix | 343-360 | 18 | |
| α-helix | 366-369 | 4 | |
| α-helix | 370-372 | 3 | |
| α-helix | 373-414 | 42 | |
| α-helix | 420-431 | 12 | |
| α-helix | 433-437 | 5 | |
| α-helix | 445-466 | 22 | |
| α-helix | 471-478 | 8 | |
| α-helix | 484-490 | 7 | |
| α-helix | 504-506 | 3 | |
| α-helix | 511-515 | 5 | |
| α-helix | 518-535 | 18 | |
| α-helix | 542-558 | 17 | |
| α-helix | 566-581 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serum albumin | A, B | protein | 585 | Homo sapiens | P02768 (AlphaFold model) |
>1AO6_1 SERUM ALBUMIN (chains A, B) DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAE NCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEV DVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLP KLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTK VHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPA DLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKC CAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVST PTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTES LVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKAT KEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL
Crystal structure of human serum albumin at 2.5 A resolution. Sugio, S., Kashima, A., Mochizuki, S. et al. Protein Eng (1999) 12:439-446. DOI 10.1093/protein/12.6.439 · PubMed
Other PDB entries of the same protein (UniProt P02768 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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