Crystal structure of the Fab fragment of an anti-DR5 antibody bound to DR5. Determined by X-ray diffraction at 3.2 Å resolution. Released 5 Feb 2014.
Explore 4OD2 in 3D Show helices and sheets RCSB PDB PDBe
4OD2 contains 15 α-helices and 59 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 | 4 | 1 | 1 |
| β-strand | 8-12 | 5 | 2 |
| β-strand | 17-22 | 6 | 1 |
| β-strand | 29 | 1 | 3 |
| β-strand | 33-36 | 4 | 2 |
| β-strand | 43-46 | 4 | 2 |
| β-strand | 47 | 1 | 4 |
| β-strand | 51 | 1 | 4 |
| β-strand | 60-65 | 6 | 1 |
| β-strand | 68-73 | 6 | 1 |
| α-helix | 78-80 | 3 | |
| β-strand | 82-86 | 5 | 2 |
| β-strand | 87-89 | 3 | 5 |
| β-strand | 96-98 | 3 | 5 |
| β-strand | 102-107 | 6 | 2 |
| α-helix | 110-111 | 2 | |
| β-strand | 112 | 1 | 6 |
| β-strand | 115-119 | 5 | 7 |
| α-helix | 120-122 | 3 | |
| α-helix | 123-126 | 4 | |
| β-strand | 131-140 | 10 | 7 |
| β-strand | 141 | 1 | 6 |
| β-strand | 145-151 | 7 | 8 |
| β-strand | 154-155 | 2 | 8 |
| β-strand | 160-162 | 3 | 7 |
| β-strand | 166-167 | 2 | 7 |
| β-strand | 173-181 | 9 | 7 |
| α-helix | 183-187 | 5 | |
| β-strand | 192-198 | 7 | 8 |
| β-strand | 201-207 | 7 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 9 |
| β-strand | 10-12 | 3 | 10 |
| β-strand | 18-25 | 8 | 9 |
| β-strand | 34-40 | 7 | 10 |
| β-strand | 43-51 | 9 | 10 |
| β-strand | 58-60 | 3 | 10 |
| β-strand | 68-73 | 6 | 9 |
| β-strand | 78-83 | 6 | 9 |
| β-strand | 92-99 | 8 | 10 |
| β-strand | 108-111 | 4 | 10 |
| β-strand | 115-119 | 5 | 10 |
| β-strand | 125 | 1 | 11 |
| β-strand | 128-132 | 5 | 12 |
| β-strand | 144-153 | 10 | 12 |
| β-strand | 154 | 1 | 11 |
| β-strand | 159-162 | 4 | 13 |
| α-helix | 163-165 | 3 | |
| β-strand | 171-173 | 3 | 12 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 12 |
| β-strand | 184-192 | 9 | 12 |
| α-helix | 194-197 | 4 | |
| β-strand | 203-208 | 6 | 13 |
| α-helix | 209-211 | 3 | |
| β-strand | 213-218 | 6 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 24 | 1 | 14 |
| β-strand | 27 | 1 | 14 |
| β-strand | 28 | 1 | 15 |
| α-helix | 29 | 1 | |
| β-strand | 32-34 | 3 | 16 |
| β-strand | 41-43 | 3 | 16 |
| α-helix | 44-45 | 2 | |
| β-strand | 49-50 | 2 | 17 |
| β-strand | 55 | 1 | 15 |
| α-helix | 60 | 1 | |
| β-strand | 61-62 | 2 | 17 |
| α-helix | 63-64 | 2 | |
| β-strand | 66 | 1 | 3 |
| β-strand | 70-74 | 5 | 18 |
| β-strand | 83-86 | 4 | 18 |
| β-strand | 90-91 | 2 | 19 |
| β-strand | 101-102 | 2 | 19 |
| α-helix | 103-104 | 2 | |
| α-helix | 107-108 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fab fragment of drozitumab, light chain | A | protein | 213 | Homo sapiens | |
| Fab fragment of drozitumab, heavy chain | B | protein | 232 | Homo sapiens | |
| Tumor necrosis factor receptor superfamily member 10B | S | protein | 111 | Homo sapiens | O14763 (AlphaFold model) |
>4OD2_1 Fab fragment of drozitumab, light chain (chains A) SELTQDPAVSVALGQTVRITCSGDSLRSYYASWYQQKPGQAPVLVIYGANNRPSGIPDRF SGSSSGNTASLTITGAQAEDEADYYCNSADSSGNHVVFGGGTKLTVLGQPKAAPSVTLFP PSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLS LTPEQWKSHKSYSCQVTHEGSTVEKTVAPTECS
>4OD2_2 Fab fragment of drozitumab, heavy chain (chains B) EVQLVQSGGGVERPGGSLRLSCAASGFTFDDYAMSWVRQAPGKGLEWVSGINWQGGSTGY ADSVKGRVTISRDNAKNSLYLQMNSLRAEDTAVYYCAKILGAGRGWYFDYWGKGTTVTVS SASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS SGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTAAP
>4OD2_3 Tumor necrosis factor receptor superfamily member 10B (chains S) RSSPSEGLCPPGHHISEDGRDCISCKYGQDYSTHWNDLLFCLRCTRCDSGEVELSPCTTT RNTVCQCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPWSDIECVHKES
Structural and functional analysis of the interaction between the agonistic monoclonal antibody Apomab and the proapoptotic receptor DR5. Adams, C., Totpal, K., Lawrence, D. et al. Cell Death Differ (2008) 15:751-761. DOI 10.1038/sj.cdd.4402306 · PubMed
Other PDB entries of the same protein (UniProt O14763 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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