Cryo-EM structure of human alpha-fetoprotein. Determined by electron microscopy at 3.31 Å resolution. Released 15 May 2024.
Explore 8X1N in 3D Show helices and sheets RCSB PDB PDBe
8X1N contains 31 α-helices and 0 β-strands across 1 chain. 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 | 43-54 | 12 | |
| α-helix | 60-74 | 15 | |
| α-helix | 86-89 | 4 | |
| α-helix | 91-98 | 8 | |
| α-helix | 102-108 | 7 | |
| α-helix | 118-127 | 10 | |
| α-helix | 147-153 | 7 | |
| α-helix | 155-169 | 15 | |
| α-helix | 175-192 | 18 | |
| α-helix | 198-246 | 49 | |
| α-helix | 252-270 | 19 | |
| α-helix | 274-290 | 17 | |
| α-helix | 297-302 | 6 | |
| α-helix | 307-316 | 10 | |
| α-helix | 317-319 | 3 | |
| α-helix | 321-323 | 3 | |
| α-helix | 344-361 | 18 | |
| α-helix | 367-384 | 18 | |
| α-helix | 390-400 | 11 | |
| α-helix | 403-422 | 20 | |
| α-helix | 424-438 | 15 | |
| α-helix | 444-461 | 18 | |
| α-helix | 468-490 | 23 | |
| α-helix | 495-501 | 7 | |
| α-helix | 508-512 | 5 | |
| α-helix | 523-526 | 4 | |
| α-helix | 528-531 | 4 | |
| α-helix | 536-539 | 4 | |
| α-helix | 543-559 | 17 | |
| α-helix | 565-583 | 19 | |
| α-helix | 588-607 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-fetoprotein | A | protein | 609 | Homo sapiens | P02771 (AlphaFold model) |
>8X1N_1 Alpha-fetoprotein (chains A) MKWVESIFLIFLLNFTESRTLHRNEYGIASILDSYQCTAEISLADLATIFFAQFVQEATY KEVSKMVKDALTAIEKPTGDEQSSGCLENQLPAFLEELCHEKEILEKYGHSDCCSQSEEG RHNCFLAHKKPTPASIPLFQVPEPVTSCEAYEEDRETFMNKFIYEIARRHPFLYAPTILL WAARYDKIIPSCCKAENAVECFQTKAATVTKELRESSLLNQHACAVMKNFGTRTFQAITV TKLSQKFTKVNFTEIQKLVLDVAHVHEHCCRGDVLDCLQDGEKIMSYICSQQDTLSNKIT ECCKLTTLERGQCIIHAENDEKPEGLSPNLNRFLGDRDFNQFSSGEKNIFLASFVHEYSR RHPQLAVSVILRVAKGYQELLEKCFQTENPLECQDKGEEELQKYIQESQALAKRSCGLFQ KLGEYYLQNAFLVAYTKKAPQLTSSELMAITRKMAATAATCCQLSEDKLLACGEGAADII IGHLCIRHEMTPVNPGVGQCCTSSYANRRPCFSSLVVDETYVPPAFSDDKFIFHKDLCQA QGVALQTMKQEFLINLVKQKPQITEEQLEAVIADFSGLLEKCCQGQEQEVCFAEEGQKLI SKTRAALGV
Structural characteristics of alpha-fetoprotein, including N-glycosylation, metal ion and fatty acid binding sites. Liu, K., Wu, C., Zhu, M. et al. Commun Biol (2024) 7:505-505. DOI 10.1038/s42003-024-06219-0 · PubMed
Other PDB entries of the same protein (UniProt P02771 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8X1N directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.