Lebrikizumab Fab bound to IL-13. Determined by X-ray diffraction at 1.9 Å resolution. Released 6 Feb 2013.
Explore 4I77 in 3D Show helices and sheets RCSB PDB PDBe
4I77 contains 24 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 | 3-7 | 5 | 1 |
| β-strand | 11-12 | 2 | 2 |
| α-helix | 17 | 1 | |
| β-strand | 18-25 | 8 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 3 |
| β-strand | 46-51 | 6 | 3 |
| β-strand | 57-59 | 3 | 3 |
| α-helix | 64-66 | 3 | |
| β-strand | 67-72 | 6 | 1 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 3 |
| β-strand | 100B-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 |
| β-strand | 120-124 | 5 | 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-3 | 2 | |
| β-strand | 4-7 | 4 | 7 |
| β-strand | 10-14 | 5 | 8 |
| β-strand | 19-25 | 7 | 7 |
| β-strand | 27C-27D | 2 | 9 |
| β-strand | 30-31 | 2 | 9 |
| 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 | 84-90 | 7 | 8 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 8 |
| β-strand | 102-107 | 6 | 8 |
| β-strand | 111 | 1 | 10 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 11 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 11 |
| β-strand | 140 | 1 | 10 |
| β-strand | 145-150 | 6 | 12 |
| β-strand | 153-154 | 2 | 12 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 11 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 11 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 12 |
| β-strand | 205-210 | 6 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-20 | 12 | |
| β-strand | 33-35 | 3 | 13 |
| α-helix | 44-51 | 8 | |
| α-helix | 58-60 | 3 | |
| α-helix | 61-70 | 10 | |
| β-strand | 89-91 | 3 | 13 |
| α-helix | 92-106 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lebrikizumab heavy chain | H | protein | 219 | Homo sapiens | |
| Lebrikizumab light chain | L | protein | 218 | Homo sapiens | |
| Interleukin-13 | Z | protein | 112 | Homo sapiens | P35225 (AlphaFold model) |
>4I77_1 Lebrikizumab heavy chain (chains H) QVTLRESGPALVKPTQTLTLTCTVSGFSLSAYSVNWIRQPPGKALEWLAMIWGDGKIVYN SALKSRLTISKDTSKNQVVLTMTNMDPVDTATYYCAGDGYYPYAMDNWGQGSLVTVSSAS TKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGL YSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVESK
>4I77_2 Lebrikizumab light chain (chains L) DIVMTQSPDSLSVSLGERATINCRASKSVDSYGNSFMHWYQQKPGQPPKLLIYLASNLES GVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQNNEDPRTFGGGTKVEIKRTVAAPSVF IFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS STLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>4I77_3 Interleukin-13 (chains Z) GPVPPSTALRELIEELVNITQNQKAPLCNGSMVWSINLTAGMYCAALESLINVSGCSAIE KTQRMLSGFCPHKVSAGQFSSLHVRDTKIEVAQFVKDLLLHLKKLFREGRFN
Structural Basis of Signaling Blockade by Anti-IL-13 Antibody Lebrikizumab. Ultsch, M., Bevers, J., Nakamura, G. et al. J Mol Biol (2013) 425:1330-1339. DOI 10.1016/j.jmb.2013.01.024 · PubMed
Other PDB entries of the same protein (UniProt P35225 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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