Crystal structure of mite allergen der F 1. Determined by X-ray diffraction at 2.0 Å resolution. Released 24 May 2017.
Explore 5VPK in 3D Show helices and sheets RCSB PDB PDBe
5VPK contains 35 α-helices and 54 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 |
|---|---|---|---|
| α-helix | 2 | 1 | |
| β-strand | 3 | 1 | 1 |
| α-helix | 4 | 1 | |
| β-strand | 15-16 | 2 | 1 |
| α-helix | 17-20 | 4 | |
| β-strand | 28 | 1 | 2 |
| β-strand | 33 | 1 | 3 |
| α-helix | 35-52 | 18 | |
| β-strand | 58 | 1 | 4 |
| α-helix | 60-66 | 7 | |
| β-strand | 73 | 1 | 3 |
| α-helix | 77-87 | 11 | |
| β-strand | 89 | 1 | 5 |
| β-strand | 91 | 1 | 4 |
| α-helix | 92-94 | 3 | |
| β-strand | 112 | 1 | 5 |
| β-strand | 116-119 | 4 | 1 |
| α-helix | 125-135 | 11 | |
| α-helix | 138 | 1 | |
| β-strand | 139-145 | 7 | 1 |
| α-helix | 148-152 | 5 | |
| β-strand | 160 | 1 | 1 |
| β-strand | 169-181 | 13 | 1 |
| β-strand | 184-190 | 7 | 1 |
| β-strand | 193 | 1 | 2 |
| β-strand | 199 | 1 | 1 |
| β-strand | 202-206 | 5 | 1 |
| α-helix | 211-213 | 3 | |
| β-strand | 219-222 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2 | 1 | |
| β-strand | 3 | 1 | 6 |
| α-helix | 4 | 1 | |
| β-strand | 15-16 | 2 | 6 |
| α-helix | 17-20 | 4 | |
| β-strand | 28 | 1 | 7 |
| β-strand | 33 | 1 | 8 |
| α-helix | 35-52 | 18 | |
| β-strand | 58 | 1 | 9 |
| α-helix | 60-62 | 3 | |
| α-helix | 63-67 | 5 | |
| β-strand | 73 | 1 | 8 |
| α-helix | 77-87 | 11 | |
| β-strand | 89 | 1 | 10 |
| β-strand | 91 | 1 | 9 |
| α-helix | 92-94 | 3 | |
| β-strand | 112 | 1 | 10 |
| β-strand | 116-119 | 4 | 6 |
| α-helix | 125-135 | 11 | |
| α-helix | 138 | 1 | |
| β-strand | 139-145 | 7 | 6 |
| α-helix | 148-152 | 5 | |
| β-strand | 160 | 1 | 6 |
| β-strand | 169-181 | 13 | 6 |
| β-strand | 184-190 | 7 | 6 |
| β-strand | 193 | 1 | 7 |
| β-strand | 199 | 1 | 6 |
| β-strand | 202-206 | 5 | 6 |
| α-helix | 211-213 | 3 | |
| β-strand | 219-222 | 4 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2 | 1 | |
| β-strand | 3 | 1 | 11 |
| α-helix | 4 | 1 | |
| β-strand | 15-16 | 2 | 11 |
| α-helix | 17-20 | 4 | |
| β-strand | 28 | 1 | 12 |
| β-strand | 33 | 1 | 13 |
| α-helix | 35-52 | 18 | |
| β-strand | 58 | 1 | 14 |
| α-helix | 60-62 | 3 | |
| α-helix | 63-67 | 5 | |
| β-strand | 73 | 1 | 13 |
| α-helix | 77-87 | 11 | |
| β-strand | 89 | 1 | 15 |
| β-strand | 91 | 1 | 14 |
| α-helix | 92-94 | 3 | |
| β-strand | 112 | 1 | 15 |
| β-strand | 117-119 | 3 | 11 |
| α-helix | 125-135 | 11 | |
| α-helix | 138 | 1 | |
| β-strand | 139-145 | 7 | 11 |
| α-helix | 148-152 | 5 | |
| β-strand | 160 | 1 | 11 |
| β-strand | 169-181 | 13 | 11 |
| β-strand | 184-190 | 7 | 11 |
| β-strand | 193 | 1 | 12 |
| β-strand | 199 | 1 | 11 |
| β-strand | 202-206 | 5 | 11 |
| α-helix | 211-213 | 3 | |
| β-strand | 219-221 | 3 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Der f 1 variant | A, B, C | protein | 223 | Dermatophagoides farinae | P16311 (AlphaFold model) |
>5VPK_1 Der f 1 variant (chains A, B, C) TSACRINSVNVPSELDLRSLRTVTPIRMQGGCGSCWAFSGVAATESAYLAYRNTSLDLSE QELVDCASQHGCHGDTIPRGIEYIQQNGVVEERSYPYVAREQQCRRPNSQHYGISNYCQI YPPDVKQIREALTQTHTAIAVIIGIKDLRAFQHYDGRTIIQHDNGYQPNYHAVNIVGYGS TQGVDYWIVRNSWDTTWGDSGYGYFQAGNNLMMIEQYPYVVIM
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Water and common crystallization additives (SO4) are not listed.
Crystal Structures Of Mite Allergens Der F 1 And Der P 1 Reveal Differences In Surface-Exposed Residues That May Influence Antibody Binding. Chruszcz, M., Chapman, M.D., Vailes, L.D. et al. J Mol Biol (2009) 386:520. DOI 10.1016/J.JMB.2008.12.049 · PubMed
Other PDB entries of the same protein (UniProt P16311 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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