Crystal structure of the receptor binding domain of botulinum neurotoxin D. Determined by X-ray diffraction at 1.65 Å resolution. Released 1 Sept 2010.
Explore 3OGG in 3D Show helices and sheets RCSB PDB PDBe
3OGG contains 11 α-helices and 38 β-strands across 1 chain. 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 | 864-867 | 4 | |
| β-strand | 868-871 | 4 | 1 |
| β-strand | 872-875 | 4 | 2 |
| β-strand | 878-881 | 4 | 2 |
| β-strand | 888-891 | 4 | 3 |
| β-strand | 896-897 | 2 | 1 |
| β-strand | 904-907 | 4 | 1 |
| β-strand | 914-917 | 4 | 3 |
| β-strand | 926 | 1 | 4 |
| β-strand | 931-939 | 9 | 1 |
| α-helix | 941-944 | 4 | |
| β-strand | 949-954 | 6 | 3 |
| β-strand | 961-967 | 7 | 3 |
| β-strand | 970-976 | 7 | 3 |
| β-strand | 982-988 | 7 | 3 |
| β-strand | 1003-1009 | 7 | 1 |
| β-strand | 1014-1019 | 6 | 1 |
| β-strand | 1022-1028 | 7 | 1 |
| β-strand | 1036 | 1 | 4 |
| α-helix | 1037-1038 | 2 | |
| β-strand | 1040-1043 | 4 | 3 |
| β-strand | 1055-1063 | 9 | 1 |
| α-helix | 1069-1079 | 11 | |
| β-strand | 1084 | 1 | 5 |
| β-strand | 1086 | 1 | 6 |
| β-strand | 1092 | 1 | 6 |
| α-helix | 1093 | 1 | |
| β-strand | 1094 | 1 | 7 |
| β-strand | 1098-1103 | 6 | 8 |
| β-strand | 1106 | 1 | 8 |
| β-strand | 1109-1114 | 6 | 9 |
| β-strand | 1117-1122 | 6 | 9 |
| β-strand | 1135-1139 | 5 | 8 |
| α-helix | 1143-1144 | 2 | |
| α-helix | 1147 | 1 | |
| β-strand | 1148 | 1 | 7 |
| α-helix | 1149 | 1 | |
| β-strand | 1150 | 1 | 5 |
| β-strand | 1154-1161 | 8 | 8 |
| β-strand | 1164-1170 | 7 | 8 |
| β-strand | 1188-1194 | 7 | 8 |
| α-helix | 1201-1203 | 3 | |
| β-strand | 1204-1209 | 6 | 8 |
| β-strand | 1218-1222 | 5 | 8 |
| β-strand | 1228-1235 | 8 | 8 |
| β-strand | 1245-1251 | 7 | 8 |
| α-helix | 1255-1257 | 3 | |
| α-helix | 1261-1263 | 3 | |
| β-strand | 1265-1268 | 4 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Botulinum neurotoxin type D | A | protein | 414 | Clostridium botulinum | P19321 |
>3OGG_1 Botulinum neurotoxin type D (chains A) SINDSKILSLQNKKNALVDTSGYNAEVRVGDNVQLNTIYTNDFKLSSSGDKIIVNLNNNI LYSAIYENSSVSFWIKISKDLTNSHNEYTIINSIEQNSGWKLCIRNGNIEWILQDVNRKY KSLIFDYSESLSHTGYTNKWFFVTITNNIMGYMKLYINGELKQSQKIEDLDEVKLDKTIV FGIDENIDENQMLWIRDFNIFSKELSNEDINIVYEGQILRNVIKDYWGNPLKFDTEYYII NDNYIDRYIAPESNVLVLVQYPDRSKLYTGNPITIKSVSDKNPYSRILNGDNIILHMLYN SRKYMIIRDTDTIYATQGGECSQNCVYALKLQSNLGNYGIGIFSIKNIVSKNKYCSQIFS SFRENTMLLADIYKPWRFSFKNAYTPVAVTNYETKLLSTSSFWKFISRDPGWVE
Structural analysis of the receptor binding domain of botulinum neurotoxin serotype D. Zhang, Y., Buchko, G.W., Qin, L. et al. Biochem Biophys Res Commun (2010) 401:498-503. DOI 10.1016/j.bbrc.2010.09.063 · PubMed
Other PDB entries of the same protein (UniProt P19321), best resolution first:
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