Crystal structure of Ky230 Fab in complex with circumsporozoite protein NANP5 peptide. Determined by X-ray diffraction at 1.55 Å resolution. Released 1 Nov 2023.
Explore 8FAS in 3D Show helices and sheets RCSB PDB PDBe
8FAS contains 22 α-helices and 47 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 |
|---|---|---|---|
| β-strand | 3-7 | 5 | 1 |
| β-strand | 11-12 | 2 | 2 |
| β-strand | 18-25 | 8 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-40 | 7 | 3 |
| β-strand | 44-51 | 8 | 3 |
| β-strand | 57-59 | 3 | 3 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 1 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 3 |
| α-helix | 96 | 1 | |
| α-helix | 99-100A | 3 | |
| β-strand | 100C-103 | 4 | 3 |
| β-strand | 107-109 | 3 | 3 |
| β-strand | 110-111 | 2 | 2 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 4 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 5 |
| β-strand | 131-132 | 2 | 5 |
| β-strand | 135-145 | 11 | 5 |
| β-strand | 146 | 1 | 4 |
| β-strand | 151-154 | 4 | 6 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 6 |
| β-strand | 163-165 | 3 | 5 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 5 |
| β-strand | 176-185 | 10 | 5 |
| α-helix | 186-188 | 3 | |
| β-strand | 195-200 | 6 | 6 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-210 | 6 | 6 |
| α-helix | 212-214 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 7 |
| β-strand | 10-14 | 5 | 3 |
| β-strand | 19-25 | 7 | 7 |
| β-strand | 27C | 1 | 8 |
| β-strand | 31 | 1 | 8 |
| β-strand | 33-38 | 6 | 3 |
| β-strand | 45-49 | 5 | 3 |
| β-strand | 53-54 | 2 | 3 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 7 |
| β-strand | 70-75 | 6 | 7 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 3 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 3 |
| β-strand | 102-107 | 6 | 3 |
| β-strand | 111 | 1 | 9 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 10 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 10 |
| β-strand | 140 | 1 | 9 |
| β-strand | 145-150 | 6 | 11 |
| β-strand | 153-154 | 2 | 11 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 10 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 10 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-197 | 7 | 11 |
| β-strand | 205-210 | 6 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ky230 Antibody, heavy chain | A | protein | 223 | Mus musculus | |
| Ky230 Antibody, light chain | B | protein | 219 | Mus musculus | |
| Circumsporozoite protein NANP5 peptide | C | protein | 20 | Plasmodium falciparum (isolate NF54) | P19597 (AlphaFold model) |
>8FAS_1 Ky230 Antibody, heavy chain (chains A) QVQLVESGGGVVQPGRSLRLSCAASGFTFSDYGMHWVRQAPGKGLEWVAIIWHDGSNKYY VDSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARAASSFGSGFDYWGQGTLVTVSS ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
>8FAS_2 Ky230 Antibody, light chain (chains B) DVVMTQSPLSLPVTLGQPASIFCRSSQSLVYSDGNTYLNWFQRRPGQSPRRLIYKVSDRD SGVPDRFSGSGSGTDFTLQISRVEAEDVGVYYCMQGTHWPPTFGQGTKVEIKRTVAAPSV FIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>8FAS_3 Circumsporozoite protein NANP5 peptide (chains C) NANPNANPNANPNANPNANP
Molecular determinants of cross-reactivity and potency by VH3-33 antibodies against the Plasmodium falciparum circumsporozoite protein. Thai, E., Murugan, R., Binter, S. et al. Cell Rep (2023) 42:113330-113330. DOI 10.1016/j.celrep.2023.113330 · PubMed
Other PDB entries of the same protein (UniProt P19597 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8FAS 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.