Single chain fv of C219 in complex with synthetic epitope peptide. Determined by X-ray diffraction at 2.4 Å resolution. Released 24 Nov 1999.
Explore 2AP2 in 3D Show helices and sheets RCSB PDB PDBe
2AP2 contains 17 α-helices and 48 β-strands across 4 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 | 10-12 | 3 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 30-31 | 2 | 3 |
| β-strand | 36-37 | 2 | 3 |
| β-strand | 39-44 | 6 | 2 |
| α-helix | 49-50 | 2 | |
| β-strand | 51-55 | 5 | 2 |
| β-strand | 59-60 | 2 | 2 |
| α-helix | 61 | 1 | |
| β-strand | 68-73 | 6 | 1 |
| β-strand | 76-81 | 6 | 1 |
| α-helix | 86-88 | 3 | |
| β-strand | 91-96 | 6 | 2 |
| α-helix | 102 | 1 | |
| β-strand | 103-104 | 2 | 2 |
| β-strand | 108-111 | 4 | 2 |
| β-strand | 116-118 | 3 | 4 |
| α-helix | 119-121 | 3 | |
| β-strand | 122-123 | 2 | 5 |
| β-strand | 130-136 | 7 | 4 |
| α-helix | 141-143 | 3 | |
| β-strand | 144-151 | 8 | 5 |
| β-strand | 157-164 | 8 | 5 |
| β-strand | 169-172 | 4 | 5 |
| α-helix | 174-176 | 3 | |
| β-strand | 180-185 | 6 | 4 |
| β-strand | 190-195 | 6 | 4 |
| α-helix | 200-202 | 3 | |
| β-strand | 204-212 | 9 | 5 |
| β-strand | 223 | 1 | 5 |
| β-strand | 227-230 | 4 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 0-3 | 4 | |
| β-strand | 4-7 | 4 | 6 |
| β-strand | 10-12 | 3 | 7 |
| β-strand | 19-25 | 7 | 6 |
| β-strand | 30-31 | 2 | 8 |
| β-strand | 36-37 | 2 | 8 |
| β-strand | 39-44 | 6 | 9 |
| β-strand | 51-55 | 5 | 9 |
| β-strand | 59-60 | 2 | 9 |
| β-strand | 68-73 | 6 | 6 |
| β-strand | 76-81 | 6 | 6 |
| β-strand | 91-96 | 6 | 9 |
| α-helix | 102 | 1 | |
| β-strand | 103-104 | 2 | 9 |
| β-strand | 109-111 | 3 | 7 |
| β-strand | 115-118 | 4 | 10 |
| α-helix | 119-121 | 3 | |
| β-strand | 122-123 | 2 | 11 |
| β-strand | 130-137 | 8 | 10 |
| α-helix | 141-143 | 3 | |
| β-strand | 144-151 | 8 | 11 |
| β-strand | 157-164 | 8 | 11 |
| β-strand | 169-172 | 4 | 11 |
| α-helix | 174-176 | 3 | |
| β-strand | 180-185 | 6 | 10 |
| α-helix | 186-188 | 3 | |
| β-strand | 190-195 | 6 | 10 |
| α-helix | 200-202 | 3 | |
| β-strand | 204-212 | 9 | 11 |
| β-strand | 222-223 | 2 | 11 |
| β-strand | 227-230 | 4 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-10 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-12 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Single chain fv | A, C | protein | 271 | Mus musculus | Q505N9 (AlphaFold model), Q6KB05 (AlphaFold model) |
| P-glycoprotein | P, Q | protein | 14 | Cricetulus griseus | P21448 (AlphaFold model) |
>2AP2_1 SINGLE CHAIN FV (chains A, C) FVRDIVMTQSPSSLTVTAGEKVTMSCKSSQSLLNSGNQKNYLTWYQQKPGQPPKLLIYWA STRESGVPDRFTGSGSGTDFTLTISSVQAEDLAVYYCQNDYSYPLTFGAGTKLEPGGGGS GGGGSGKSGGGGEVQLQQSGAELVRPGASVKLSCTASGFNIKDDFMHWVKQRPEQGLEWI GRIDPANDNTKYAPKFQDKATIIADTSSNTAYLQLSSLTSEDTAVYYCARREVYSYYSPL DVWGAGTTVTVPSGSEQKLISEEDLNHHHHH
>2AP2_2 P-GLYCOPROTEIN (chains P, Q) VVQEALDKAREGRT
Antibody C219 recognizes an alpha-helical epitope on P-glycoprotein. van Den Elsen, J.M., Kuntz, D.A., Hoedemaeker, F.J. et al. Proc Natl Acad Sci U S A (1999) 96:13679-13684. DOI 10.1073/pnas.96.24.13679 · PubMed
Other PDB entries of the same protein (UniProt Q505N9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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