Fusobacterium nucleatum adhesin CbpF. Determined by electron microscopy at 3.8 Å resolution. Released 2 Apr 2025.
Explore 9GH4 in 3D Show helices and sheets RCSB PDB PDBe
9GH4 contains 15 α-helices and 81 β-strands across 3 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 |
|---|---|---|---|
| β-strand | 28-31 | 4 | 1 |
| β-strand | 38-42 | 5 | 1 |
| β-strand | 45-46 | 2 | 1 |
| β-strand | 52-56 | 5 | 1 |
| β-strand | 59-60 | 2 | 1 |
| β-strand | 66-70 | 5 | 1 |
| β-strand | 73-74 | 2 | 1 |
| β-strand | 80-84 | 5 | 1 |
| β-strand | 87-88 | 2 | 1 |
| β-strand | 93-98 | 6 | 1 |
| β-strand | 101-102 | 2 | 1 |
| β-strand | 107-116 | 10 | 1 |
| β-strand | 122-130 | 9 | 1 |
| β-strand | 136-140 | 5 | 1 |
| β-strand | 143 | 1 | 2 |
| β-strand | 147 | 1 | 2 |
| β-strand | 150-151 | 2 | 1 |
| β-strand | 157-161 | 5 | 1 |
| β-strand | 164-165 | 2 | 1 |
| β-strand | 173-175 | 3 | 1 |
| β-strand | 180-181 | 2 | 1 |
| β-strand | 189-191 | 3 | 1 |
| β-strand | 202-204 | 3 | 1 |
| β-strand | 212 | 1 | 3 |
| β-strand | 213-215 | 3 | 4 |
| β-strand | 217 | 1 | 5 |
| α-helix | 218-219 | 2 | |
| β-strand | 228 | 1 | 6 |
| α-helix | 232-237 | 6 | |
| α-helix | 246-249 | 4 | |
| α-helix | 255-260 | 6 | |
| α-helix | 269-272 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cell surface protein | A, B, C | protein | 489 | Fusobacterium nucleatum | Q8RIS0 (AlphaFold model) |
>9GH4_1 Cell surface protein (chains A, B, C) MKKTAIAIAVALAGFATVAQASAAPVIKAGTATDSTEAGVDNVANGVKSSAFGYDNKAIE KESSAFGTGNRATGEFSSAFGFHNIASKIHSSAFGSNNAADGVNSSAFGFKNTVSGFNSS AFGSQYQVTGNFSGAFGMGEFNGQYQYKNEGNNSYMIGNKNKIASGSDDNFILGNNVHIG GGINNSVALGNNSTVSASNTVSVGSSTLKRKIVNVGDGAISANSSDAVTGRQLYSGNGID TAAWQNKLNVTRKNDYKDANDIDVNKWKAKLGVGSGGGGGAPVDAYTKSEADNKFANKTD LNDYTKKDDYKDANGIDVDKWKAKLGTGAGTADIENLRNEVNEKIDDVKDEVRTVGSLSA ALAGLHPMQYDPKAPVQVMAALGHYRDKQSVAVGASYYFNDRFMMSTGIALSGEKRTKTM ANVGFTLKLGKGSGVTYDETPQYVVQNEVKRLTVENQELKERVRNLEEKLNMLLKNKRSS AWSHPQFEK
Structural basis for immune cell binding of Fusobacterium nucleatum via the trimeric autotransporter adhesin CbpF. Marongiu, G.L., Fink, U., Schopf, F. et al. Proc Natl Acad Sci U S A (2025) 122:e2418155122-e2418155122. DOI 10.1073/pnas.2418155122 · PubMed
Other PDB entries of the same protein (UniProt Q8RIS0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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