Humanized antibody 4B12 Fab complexed with a CemX segment. Determined by X-ray diffraction at 1.92 Å resolution. Released 29 Jan 2014.
Explore 4LKX in 3D Show helices and sheets RCSB PDB PDBe
4LKX contains 19 α-helices and 45 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 | 3-6 | 4 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 1 |
| β-strand | 34-39 | 7 | 2 |
| β-strand | 46-52 | 7 | 2 |
| β-strand | 57-59 | 3 | 2 |
| α-helix | 64-66 | 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 | 88-96 | 9 | 2 |
| β-strand | 99-103 | 5 | 2 |
| β-strand | 107-111 | 5 | 2 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 3 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 4 |
| β-strand | 135-145 | 11 | 4 |
| β-strand | 146 | 1 | 3 |
| β-strand | 151-154 | 4 | 5 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 5 |
| β-strand | 163-165 | 3 | 4 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 4 |
| β-strand | 176-185 | 10 | 4 |
| α-helix | 186-189 | 4 | |
| β-strand | 195-200 | 6 | 5 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-210 | 6 | 5 |
| α-helix | 212-214 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 6 |
| β-strand | 10-13 | 4 | 7 |
| β-strand | 19-25 | 7 | 6 |
| β-strand | 27C | 1 | 8 |
| β-strand | 31 | 1 | 8 |
| β-strand | 33-38 | 6 | 7 |
| β-strand | 45-49 | 5 | 7 |
| β-strand | 53-54 | 2 | 7 |
| β-strand | 62-67 | 6 | 6 |
| β-strand | 70-75 | 6 | 6 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 7 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 7 |
| β-strand | 102-106 | 5 | 7 |
| 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 |
| β-strand | 173-182 | 10 | 10 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-197 | 7 | 11 |
| β-strand | 205-210 | 6 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| α-helix | 13-14 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fab fragment heavy chain | A | protein | 225 | Homo sapiens | Q6GMX6 (AlphaFold model) |
| Fab fragment light chain | B | protein | 219 | Homo sapiens | Q0KKI6 (AlphaFold model) |
| CemX segment | R | protein | 14 | Homo sapiens |
>4LKX_1 Fab fragment heavy chain (chains A) QVQLQESGPGLVKPSETLSLTCTVSGYSITSDYAWNWIRQPPGKGLEWIGSISYSGITGY NPSLKSRVTISRDTSKNQFSLKLSSVTAADTAVYYCARMGYDGLAYWGQGTLVTVSSAST KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY SLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKAEPKSCDKTHT
>4LKX_2 Fab fragment light chain (chains B) DIVMTQTPLSLSVTPGQPASISCRSSQSIVHSNGNTYLEWYLQKPGQSPQLLIYKVSNRF SGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCFQGSHVPPTFGGGTKVEIKRTVAAPSV FIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>4LKX_3 CemX segment (chains R) LAGGSAQSQRAPDR
Two potential therapeutic antibodies bind to a peptide segment of membrane-bound IgE in different conformations. Chu, H.M., Wright, J., Chan, Y.H. et al. Nat Commun (2014) 5:3139-3139. DOI 10.1038/ncomms4139 · PubMed
Other PDB entries of the same protein (UniProt Q6GMX6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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