Computational design of stable mammalian serum albumins for bacterial expression. Determined by X-ray diffraction at 2.0 Å resolution. Released 10 May 2023.
Explore 8A9Q in 3D Show helices and sheets RCSB PDB PDBe
8A9Q contains 80 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 | 6-14 | 9 | |
| α-helix | 16-30 | 15 | |
| α-helix | 36-55 | 20 | |
| α-helix | 66-75 | 10 | |
| α-helix | 80-84 | 5 | |
| α-helix | 85-92 | 8 | |
| α-helix | 97-104 | 8 | |
| α-helix | 116-119 | 4 | |
| 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 | 228-247 | 20 | |
| α-helix | 250-266 | 17 | |
| α-helix | 268-270 | 3 | |
| α-helix | 276-280 | 5 | |
| α-helix | 283-292 | 10 | |
| α-helix | 293-299 | 7 | |
| α-helix | 302-304 | 3 | |
| α-helix | 306 | 1 | |
| α-helix | 307-311 | 5 | |
| α-helix | 315-321 | 7 | |
| α-helix | 323-337 | 15 | |
| α-helix | 343-361 | 19 | |
| α-helix | 366-370 | 5 | |
| α-helix | 373-397 | 25 | |
| α-helix | 400-414 | 15 | |
| α-helix | 420-438 | 19 | |
| α-helix | 442-466 | 25 | |
| α-helix | 471-477 | 7 | |
| α-helix | 484-490 | 7 | |
| α-helix | 500-502 | 3 | |
| α-helix | 504-507 | 4 | |
| α-helix | 512-515 | 4 | |
| α-helix | 518-535 | 18 | |
| α-helix | 541-558 | 18 | |
| α-helix | 564-582 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-14 | 9 | |
| α-helix | 16-30 | 15 | |
| α-helix | 36-55 | 20 | |
| α-helix | 66-75 | 10 | |
| α-helix | 80-84 | 5 | |
| α-helix | 85-92 | 8 | |
| α-helix | 97-104 | 8 | |
| α-helix | 113-115 | 3 | |
| α-helix | 117-119 | 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 | 228-247 | 20 | |
| α-helix | 250-266 | 17 | |
| α-helix | 268-271 | 4 | |
| α-helix | 273-275 | 3 | |
| α-helix | 278-280 | 3 | |
| α-helix | 283-285 | 3 | |
| α-helix | 286-291 | 6 | |
| α-helix | 293-298 | 6 | |
| α-helix | 302-304 | 3 | |
| α-helix | 306 | 1 | |
| α-helix | 307-311 | 5 | |
| α-helix | 315-320 | 6 | |
| α-helix | 323-336 | 14 | |
| α-helix | 343-361 | 19 | |
| α-helix | 366-370 | 5 | |
| α-helix | 373-397 | 25 | |
| α-helix | 400-414 | 15 | |
| α-helix | 420-437 | 18 | |
| α-helix | 442-466 | 25 | |
| α-helix | 471-478 | 8 | |
| α-helix | 484-489 | 6 | |
| α-helix | 504-507 | 4 | |
| α-helix | 511-514 | 4 | |
| α-helix | 518-535 | 18 | |
| α-helix | 541-559 | 19 | |
| α-helix | 564-582 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Albumin | A, B | protein | 585 | Escherichia coli | P02768 (AlphaFold model) |
>8A9Q_1 Albumin (chains A, B) DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDLVKMVNEVTEFAKTCVADESAE NCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEP DVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLYFAKRYKAAFTECCQAADKAACLLP KLDELREEGKASSAKQRHKCAILQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTK VHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPA DLPSLAADFIESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKC CAAADPHECYSKVFDEFKPLIEEPQNLIKQNCELFEQLGEYKFQNALLIRYTKKVPQVST PTLVEVARNLGKVGSKCCKHPEAKRMPCAEDYLSIVLNQLCVLHEKTPVSDRVTKCCTES LVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEEERQIKKQTALVELVKHKPKAT KEQLKAVMDDFSAFVEKCCKADDKETCFAEEGKKLIAASQAALGL
Stable Mammalian Serum Albumins Designed for Bacterial Expression. Khersonsky, O., Goldsmith, M., Zaretsky, I. et al. J Mol Biol (2023) 435:168191-168191. DOI 10.1016/j.jmb.2023.168191 · 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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