MGG4 Fab in complex with peptide. Determined by X-ray diffraction at 1.77 Å resolution. Released 7 Mar 2018.
Explore 6BQB in 3D Show helices and sheets RCSB PDB PDBe
6BQB contains 19 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 | 10-12 | 3 | 8 |
| β-strand | 18-25 | 8 | 7 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 8 |
| β-strand | 45-51 | 7 | 8 |
| β-strand | 57-59 | 3 | 8 |
| β-strand | 64 | 1 | 7 |
| β-strand | 67-72 | 6 | 7 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 7 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-93 | 6 | 8 |
| β-strand | 103 | 1 | 8 |
| β-strand | 107-111 | 5 | 8 |
| α-helix | 114-116 | 3 | |
| β-strand | 117 | 1 | 9 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 10 |
| α-helix | 125-127 | 3 | |
| α-helix | 130-131 | 2 | |
| β-strand | 135-145 | 11 | 10 |
| β-strand | 146 | 1 | 9 |
| β-strand | 151-154 | 4 | 11 |
| α-helix | 155-157 | 3 | |
| β-strand | 163-165 | 3 | 10 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 10 |
| β-strand | 176-185 | 10 | 10 |
| α-helix | 186-188 | 3 | |
| β-strand | 195-200 | 6 | 11 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-210 | 6 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 27C | 1 | 3 |
| β-strand | 31 | 1 | 3 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| β-strand | 98 | 1 | 2 |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 111 | 1 | 4 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 5 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 5 |
| β-strand | 140 | 1 | 4 |
| β-strand | 145-150 | 6 | 6 |
| β-strand | 153-154 | 2 | 6 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 5 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 5 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-197 | 7 | 6 |
| β-strand | 205-210 | 6 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MGG4 Fab light chain | L | protein | 220 | Homo sapiens | |
| MGG4 Fab heavy chain | H | protein | 224 | Homo sapiens | |
| N-terminal junction peptide | P | protein | 16 | Plasmodium falciparum | Q7K740 (AlphaFold model) |
>6BQB_1 MGG4 Fab light chain (chains L) DIVMTQSPDSLAVSLGERATINCRSSQSVLSSSNNKNYLAWYQHKPRQPPKLLIYWASTR ESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYTASPFFGGGTKVEIKRTVAAPS VFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYS LSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>6BQB_2 MGG4 Fab heavy chain (chains H) QVQLVESGGGVVQPGRSLRLSCAASGFRFSDYGMHWVRQAPGKGLEWVALIWYDGSNESY LDSVKGRFTISRDNSKNTLYLQMNNLRTEDTAVYYCAKLLVGITTDVFDVWGQGTVVTVS SASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS SGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC
>6BQB_3 N-terminal junction peptide (chains P) XKQPADGNPDPNANPX
A public antibody lineage that potently inhibits malaria infection through dual binding to the circumsporozoite protein. Tan, J., Sack, B.K., Oyen, D. et al. Nat Med (2018) 24:401-407. DOI 10.1038/nm.4513 · PubMed
Other PDB entries of the same protein (UniProt Q7K740 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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