The structure of the anti-c-myc antibody 9E10 Fab fragment/epitope peptide complex reveals a novel binding mode dominated by the heavy chain hypervariable loops. Determined by X-ray diffraction at 2.7 Å resolution. Released 12 Feb 2008.
Explore 2OR9 in 3D Show helices and sheets RCSB PDB PDBe
2OR9 contains 29 α-helices and 96 β-strands across 5 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 | 8 |
| β-strand | 10-12 | 3 | 4 |
| β-strand | 16-25 | 10 | 8 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 4 |
| β-strand | 45-51 | 7 | 4 |
| β-strand | 57-58 | 2 | 4 |
| β-strand | 64 | 1 | 8 |
| β-strand | 67-72 | 6 | 8 |
| β-strand | 77-82C | 9 | 8 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-100 | 13 | 4 |
| β-strand | 100C-103 | 11 | 4 |
| β-strand | 107-111 | 5 | 4 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 9 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 10 |
| β-strand | 135-145 | 11 | 10 |
| β-strand | 146 | 1 | 9 |
| β-strand | 153-154 | 2 | 11 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 11 |
| β-strand | 163-165 | 3 | 10 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 10 |
| β-strand | 175-184 | 10 | 10 |
| β-strand | 194-196 | 3 | 11 |
| α-helix | 200-202 | 3 | |
| β-strand | 207-209 | 3 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 18 |
| β-strand | 10-12 | 3 | 19 |
| β-strand | 18-25 | 8 | 18 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 19 |
| β-strand | 45-51 | 7 | 19 |
| β-strand | 57-58 | 2 | 19 |
| β-strand | 64 | 1 | 18 |
| β-strand | 67-72 | 6 | 18 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 18 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 19 |
| β-strand | 96-100A | 6 | 20 |
| β-strand | 100D-100I | 6 | 20 |
| β-strand | 103 | 1 | 19 |
| β-strand | 107-111 | 5 | 19 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 21 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 22 |
| β-strand | 135-145 | 11 | 22 |
| β-strand | 146 | 1 | 21 |
| β-strand | 153-154 | 2 | 23 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 23 |
| β-strand | 163-165 | 3 | 22 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 22 |
| β-strand | 175-184 | 10 | 22 |
| β-strand | 194-199 | 6 | 23 |
| α-helix | 200-202 | 3 | |
| β-strand | 204-209 | 6 | 23 |
| 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-28 | 3 | 3 |
| β-strand | 30-31 | 2 | 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 |
| β-strand | 84-90 | 7 | 2 |
| β-strand | 97 | 1 | 4 |
| β-strand | 98 | 1 | 2 |
| α-helix | 99 | 1 | |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 111 | 1 | 5 |
| β-strand | 114-118 | 5 | 6 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 6 |
| β-strand | 140 | 1 | 5 |
| β-strand | 144-150 | 7 | 7 |
| β-strand | 153-155 | 3 | 7 |
| β-strand | 159-163 | 5 | 6 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 6 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-198 | 8 | 7 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 12 |
| β-strand | 10-14 | 5 | 13 |
| β-strand | 19-25 | 7 | 12 |
| β-strand | 27C-27D | 2 | 14 |
| β-strand | 30-31 | 2 | 14 |
| β-strand | 33-38 | 6 | 13 |
| β-strand | 45-49 | 5 | 13 |
| β-strand | 53-54 | 2 | 13 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 12 |
| β-strand | 70-75 | 6 | 12 |
| β-strand | 84-90 | 7 | 13 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 13 |
| β-strand | 102-107 | 6 | 13 |
| β-strand | 111 | 1 | 15 |
| β-strand | 114-118 | 5 | 16 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 16 |
| β-strand | 140 | 1 | 15 |
| β-strand | 144-150 | 7 | 17 |
| β-strand | 153-154 | 2 | 17 |
| β-strand | 159-163 | 5 | 16 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 16 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-198 | 8 | 17 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-5 | 4 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Monoclonal anti-c-myc antibody 9E10 | L, M | protein | 218 | Mus musculus | P01654 (AlphaFold model) |
| Monoclonal anti-c-myc antibody 9E10 | H, I | protein | 228 | Mus musculus | |
| synthetic epitope peptide of 9E10 | P | protein | 11 | P01106 (AlphaFold model) |
>2OR9_1 Monoclonal anti-c-myc antibody 9E10 (chains L, M) DIVLTQSPASLAVSLGQRATISCRASESVDNYGFSFMNWFQQKPGQPPKLLIYAISNRGS GVPARFSGSGSGTDFSLNIHPVEEDDPAMYFCQQTKEVPWTFGGGTKLEIKRADAAPTVS IFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMS STLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>2OR9_2 Monoclonal anti-c-myc antibody 9E10 (chains H, I) EVHLVESGGDLVKPGGSLKLSCAASGFTFSHYGMSWVRQTPDKRLEWVATIGSRGTYTHY PDSVKGRFTISRDNDKNALYLQMNSLKSEDTAMYYCARRSEFYYYGNTYYYSAMDYWGQG ASVTVSSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTF PAVLQSDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRD
>2OR9_3 synthetic epitope peptide of 9E10 (chains P) EQKLISEEDLN
The structure of the anti-c-myc antibody 9E10 Fab fragment/epitope peptide complex reveals a novel binding mode dominated by the heavy chain hypervariable loops. Krauss, N., Wessner, H., Welfle, K. et al. Proteins (2008) 73:552-565. DOI 10.1002/prot.22080 · PubMed
Other PDB entries of the same protein (UniProt P01654 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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