Crystal structure of Fab364 in complex with NPNA2 peptide from circumsporozoite protein. Determined by X-ray diffraction at 2.09 Å resolution. Released 29 Jul 2020.
Explore 6WFW in 3D Show helices and sheets RCSB PDB PDBe
6WFW contains 17 α-helices and 48 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 | 6-13 | 8 | 1 |
| β-strand | 17-25 | 9 | 1 |
| α-helix | 28-41 | 14 | |
| β-strand | 46-51 | 6 | 1 |
| β-strand | 56-61 | 6 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 2 |
| β-strand | 11-12 | 2 | 3 |
| β-strand | 17-25 | 9 | 2 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 4 |
| β-strand | 45-51 | 7 | 4 |
| β-strand | 57-59 | 3 | 4 |
| β-strand | 67-72 | 6 | 2 |
| β-strand | 77-82A | 7 | 2 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 4 |
| α-helix | 96 | 1 | |
| β-strand | 100B-103 | 4 | 4 |
| β-strand | 107-109 | 3 | 4 |
| β-strand | 110-111 | 2 | 3 |
| β-strand | 116 | 1 | 5 |
| α-helix | 117-118 | 2 | |
| β-strand | 119-123 | 5 | 6 |
| β-strand | 134-144 | 11 | 6 |
| β-strand | 145 | 1 | 5 |
| β-strand | 150-153 | 4 | 1 |
| α-helix | 154-156 | 3 | |
| β-strand | 158 | 1 | 1 |
| β-strand | 162-164 | 3 | 6 |
| α-helix | 165-167 | 3 | |
| β-strand | 168-169 | 2 | 6 |
| β-strand | 175-184 | 10 | 6 |
| α-helix | 185-189 | 5 | |
| β-strand | 194-199 | 6 | 1 |
| α-helix | 200-202 | 3 | |
| β-strand | 204-209 | 6 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 7 |
| β-strand | 10-13 | 4 | 8 |
| β-strand | 19-25 | 7 | 7 |
| β-strand | 33-38 | 6 | 8 |
| β-strand | 45-49 | 5 | 8 |
| β-strand | 53-54 | 2 | 8 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 7 |
| β-strand | 70-75 | 6 | 7 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 8 |
| β-strand | 97-98 | 2 | 8 |
| β-strand | 102-106 | 5 | 8 |
| β-strand | 111 | 1 | 9 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 10 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| 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 | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 11 |
| β-strand | 205-210 | 6 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Immunoglobulin G-binding protein G | G | protein | 60 | Streptococcus sp. group G | P19909 (AlphaFold model) |
| Fab364 heavy chain | H | protein | 219 | Homo sapiens | |
| Fab364 light chain | L | protein | 211 | Homo sapiens | |
| NPNA2 peptide | P | protein | 8 | Plasmodium falciparum | P02893 (AlphaFold model) |
>6WFW_1 Immunoglobulin G-binding protein G (chains G) PAVTTYKLVINGKTLKGETTTKAVDAETAEKAFKQYANDNGVDGVWTYDDATKTFTVTEH
>6WFW_2 Fab364 heavy chain (chains H) QVQLVESGGGVVQPXGSLRLSCAASGFTFSGYGMHWVRQVPGKGLEWVAIIWFDGSQKYY ADSVQGRFTISRDNXKKTLFLRMNSLRAEDTAVYYCAKVHDDEPTQDYWGQGTLVTVFNQ IKGPSVFPLAPSXXXXXSGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGL YSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK
>6WFW_3 Fab364 light chain (chains L) IQMTQSPSTLSASVGDRVTITCRASQGISTSLAWYQQKPGKAPKLLIYKASSLESGVPSR FSGSGSGTEFTLTITSLQPEDFATYYCQQYKRYWTFGQGTKVEIKRTVAAPSVFIFPPSD EQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLS KADYEKHKVYACEVTHQGLSSPVTKSFNRGE
>6WFW_4 NPNA2 peptide (chains P) NPNANPNA
Structural and biophysical correlation of anti-NANP antibodies with in vivo protection against P. falciparum. Pholcharee, T., Oyen, D., Flores-Garcia, Y. et al. Nat Commun (2021) 12:1063-1063. DOI 10.1038/s41467-021-21221-4 · PubMed
Other PDB entries of the same protein (UniProt P19909 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6WFW 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.