Three-dimensional structure of a human FAB with high affinity for tetanus toxoid. Determined by X-ray diffraction at 1.84 Å resolution. Released 4 Feb 1998.
Explore 1AQK in 3D Show helices and sheets RCSB PDB PDBe
1AQK contains 15 α-helices and 45 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 | 7 |
| β-strand | 11-12 | 2 | 8 |
| β-strand | 18-25 | 8 | 7 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 9 |
| β-strand | 45-51 | 7 | 9 |
| β-strand | 58-60 | 3 | 9 |
| β-strand | 68-73 | 6 | 7 |
| β-strand | 78-83 | 6 | 7 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 9 |
| β-strand | 110-113 | 4 | 9 |
| β-strand | 117-119 | 3 | 9 |
| β-strand | 120-121 | 2 | 8 |
| β-strand | 127 | 1 | 10 |
| α-helix | 128-129 | 2 | |
| β-strand | 130-134 | 5 | 11 |
| α-helix | 138-140 | 3 | |
| β-strand | 145-155 | 11 | 11 |
| β-strand | 156 | 1 | 10 |
| β-strand | 161-164 | 4 | 12 |
| α-helix | 165-167 | 3 | |
| β-strand | 174-175 | 2 | 11 |
| α-helix | 176-178 | 3 | |
| β-strand | 179-180 | 2 | 11 |
| β-strand | 186-195 | 10 | 11 |
| β-strand | 204-210 | 7 | 12 |
| α-helix | 211-213 | 3 | |
| β-strand | 215-221 | 7 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 1 |
| β-strand | 9-12 | 4 | 2 |
| β-strand | 18-23 | 6 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 36-40 | 5 | 2 |
| β-strand | 47-50 | 4 | 2 |
| β-strand | 51 | 1 | 3 |
| β-strand | 55 | 1 | 3 |
| β-strand | 64-69 | 6 | 1 |
| β-strand | 72-77 | 6 | 1 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-93 | 8 | 2 |
| β-strand | 99-101 | 3 | 2 |
| β-strand | 105-109 | 5 | 2 |
| β-strand | 115 | 1 | 4 |
| α-helix | 116-117 | 2 | |
| β-strand | 118-122 | 5 | 5 |
| α-helix | 123-125 | 3 | |
| α-helix | 126-130 | 5 | |
| β-strand | 134-143 | 10 | 5 |
| β-strand | 144 | 1 | 4 |
| β-strand | 149-154 | 6 | 6 |
| β-strand | 157-158 | 2 | 6 |
| α-helix | 159 | 1 | |
| β-strand | 163-165 | 3 | 5 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 5 |
| β-strand | 176-184 | 9 | 5 |
| α-helix | 186-191 | 6 | |
| β-strand | 195-201 | 7 | 6 |
| β-strand | 204-210 | 7 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| FAB B7-15A2 | L | protein | 216 | Homo sapiens | P0DOY2 (AlphaFold model) |
| FAB B7-15A2 | H | protein | 226 | Homo sapiens | P01857 (AlphaFold model) |
>1AQK_1 FAB B7-15A2 (chains L) QNVLTQPPSVSGAPGQRVTISCTGSNSNIGAGFTVHWYQHLPGTAPKLLIFANTNRPSGV PDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDSSLSARFGGGTRLTVLGQPKAAPSVT LFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVNAGVETTKPSKQSNNKYAASS YLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPAECS
>1AQK_2 FAB B7-15A2 (chains H) QVQLVESGGGVVQPGRSLRLSCAASGFTFNNYAIHWVRQAPGKGLEWVAFISYDGSKNYY ADSVKGRFTISRDNSKNTLFLQMNSLRPEDTAIYYCARVLFQQLVLYAPFDIWGQGTMVT VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPQPVTVSWNSGALTSGVHTFPAVL QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
Three-dimensional structure of a human Fab with high affinity for tetanus toxoid. Faber, C., Shan, L., Fan, Z. et al. Immunotechnology (1998) 3:253-270. DOI 10.1016/S1380-2933(97)10003-3 · PubMed
Other PDB entries of the same protein (UniProt P0DOY2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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