The three-dimensional structure of an engineered scFv T84.66 dimer or diabody in VL to VH linkage. Determined by X-ray diffraction at 2.6 Å resolution. Released 18 Mar 2003.
Explore 1MOE in 3D Show helices and sheets RCSB PDB PDBe
1MOE contains 13 α-helices and 46 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 | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 30-31 | 2 | 3 |
| β-strand | 34-35 | 2 | 3 |
| β-strand | 37-42 | 6 | 2 |
| β-strand | 49-53 | 5 | 2 |
| β-strand | 57-58 | 2 | 2 |
| α-helix | 59 | 1 | |
| β-strand | 66-71 | 6 | 1 |
| β-strand | 74-79 | 6 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 2 |
| β-strand | 102 | 1 | 2 |
| β-strand | 106-110 | 5 | 2 |
| β-strand | 122-125 | 4 | 4 |
| α-helix | 126-128 | 3 | |
| β-strand | 129-131 | 3 | 5 |
| β-strand | 137-144 | 8 | 4 |
| α-helix | 148-150 | 3 | |
| β-strand | 153-158 | 6 | 5 |
| β-strand | 165-171 | 7 | 5 |
| β-strand | 176-179 | 4 | 5 |
| α-helix | 181-183 | 3 | |
| β-strand | 187-192 | 6 | 4 |
| β-strand | 197-202 | 6 | 4 |
| α-helix | 207-209 | 3 | |
| β-strand | 211-217 | 7 | 5 |
| β-strand | 234-238 | 5 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 6 |
| β-strand | 10-13 | 4 | 7 |
| β-strand | 19-25 | 7 | 6 |
| β-strand | 30-31 | 2 | 8 |
| β-strand | 34-35 | 2 | 8 |
| β-strand | 37-42 | 6 | 7 |
| β-strand | 48-53 | 6 | 7 |
| β-strand | 57-58 | 2 | 7 |
| α-helix | 59 | 1 | |
| β-strand | 66-70 | 5 | 6 |
| β-strand | 74-79 | 6 | 6 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 7 |
| α-helix | 100 | 1 | |
| β-strand | 101-102 | 2 | 7 |
| β-strand | 106-110 | 5 | 7 |
| β-strand | 122-125 | 4 | 9 |
| α-helix | 126-128 | 3 | |
| β-strand | 129-131 | 3 | 10 |
| β-strand | 137-144 | 8 | 9 |
| α-helix | 148-150 | 3 | |
| β-strand | 153-158 | 6 | 10 |
| β-strand | 164-170 | 7 | 10 |
| β-strand | 177-179 | 3 | 10 |
| α-helix | 181-183 | 3 | |
| β-strand | 187-192 | 6 | 9 |
| β-strand | 197-202 | 6 | 9 |
| α-helix | 207-209 | 3 | |
| β-strand | 211-217 | 7 | 10 |
| β-strand | 234-238 | 5 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| anti-CEA mAb T84.66 | A, B | protein | 240 | Mus musculus | P01660 (AlphaFold model) |
>1MOE_1 anti-CEA mAb T84.66 (chains A, B) DIVLTQSPASLAVSLGQRATMSCRAGESVDIFGVGFLHWYQQKPGQPPKLLIYRASNLES GIPVRFSGTGSRTDFTLIIDPVEADDVATYYCQQTNEDPYTFGGGTKLEIKGGGSGGGGE VQLQQSGAELVEPGASVKLSCTASGFNIKDTYMHWVKQRPEQGLEWIGRIDPANGNSKYV PKFQGKATITADTSSNTAYLQLTSLTSEDTAVYYCAPFGYYVSDYAMAYWGQGTSVTVSS
The Crystal Structure of an Anti-CEA scFv Diabody Assembled from T84.66 scFvs in VL-to-VH Orientation: Implications for Diabody Flexibility. Carmichael, J.A., Power, B.E., Garrett, T.P. et al. J Mol Biol (2003) 326:341-351. DOI 10.1016/S0022-2836(02)01428-6 · PubMed
Other PDB entries of the same protein (UniProt P01660 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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