Crystal structure of the receptor binding domain. Determined by X-ray diffraction at 3.1 Å resolution. Released 28 Dec 2011.
Explore 3AZV in 3D Show helices and sheets RCSB PDB PDBe
3AZV contains 21 α-helices and 71 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 |
|---|---|---|---|
| α-helix | 859-866 | 8 | |
| β-strand | 868-875 | 8 | 1 |
| β-strand | 878-881 | 4 | 1 |
| β-strand | 888-892 | 5 | 2 |
| β-strand | 896-897 | 2 | 1 |
| β-strand | 905-908 | 4 | 1 |
| β-strand | 916-920 | 5 | 2 |
| α-helix | 923-929 | 7 | |
| β-strand | 933-943 | 11 | 1 |
| α-helix | 949-951 | 3 | |
| β-strand | 952-958 | 7 | 2 |
| β-strand | 963-969 | 7 | 2 |
| β-strand | 972-978 | 7 | 2 |
| β-strand | 984-990 | 7 | 2 |
| β-strand | 1004-1011 | 8 | 1 |
| β-strand | 1015-1020 | 6 | 1 |
| β-strand | 1023-1029 | 7 | 1 |
| α-helix | 1030-1032 | 3 | |
| β-strand | 1041-1048 | 8 | 2 |
| β-strand | 1063-1072 | 10 | 1 |
| α-helix | 1078-1087 | 10 | |
| β-strand | 1093 | 1 | 3 |
| β-strand | 1095 | 1 | 4 |
| β-strand | 1101 | 1 | 4 |
| α-helix | 1102 | 1 | |
| β-strand | 1103 | 1 | 5 |
| β-strand | 1107-1112 | 6 | 6 |
| α-helix | 1113-1115 | 3 | |
| β-strand | 1118-1123 | 6 | 6 |
| β-strand | 1126-1131 | 6 | 6 |
| β-strand | 1144-1150 | 7 | 6 |
| β-strand | 1157 | 1 | 5 |
| β-strand | 1159 | 1 | 3 |
| β-strand | 1163-1169 | 7 | 6 |
| β-strand | 1174-1179 | 6 | 6 |
| β-strand | 1190-1192 | 3 | 7 |
| β-strand | 1193-1196 | 4 | 6 |
| α-helix | 1200-1206 | 7 | |
| β-strand | 1209-1215 | 7 | 6 |
| β-strand | 1220-1226 | 7 | 6 |
| β-strand | 1227 | 1 | 8 |
| β-strand | 1234 | 1 | 8 |
| β-strand | 1236-1245 | 10 | 7 |
| β-strand | 1255-1264 | 10 | 7 |
| α-helix | 1270-1272 | 3 | |
| α-helix | 1274-1276 | 3 | |
| β-strand | 1278-1282 | 5 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 859-866 | 8 | |
| β-strand | 868-875 | 8 | 9 |
| β-strand | 878-881 | 4 | 9 |
| β-strand | 888-892 | 5 | 10 |
| β-strand | 897 | 1 | 9 |
| β-strand | 905-908 | 4 | 9 |
| β-strand | 916-920 | 5 | 10 |
| α-helix | 923-931 | 9 | |
| β-strand | 934-942 | 9 | 9 |
| α-helix | 949-951 | 3 | |
| β-strand | 952-958 | 7 | 10 |
| β-strand | 963-969 | 7 | 10 |
| β-strand | 972-978 | 7 | 10 |
| β-strand | 984-990 | 7 | 10 |
| β-strand | 1004-1010 | 7 | 9 |
| β-strand | 1016-1020 | 5 | 9 |
| β-strand | 1023-1028 | 6 | 9 |
| α-helix | 1037-1039 | 3 | |
| β-strand | 1041-1048 | 8 | 10 |
| α-helix | 1049-1050 | 2 | |
| β-strand | 1063-1072 | 10 | 9 |
| α-helix | 1078-1087 | 10 | |
| β-strand | 1093 | 1 | 11 |
| β-strand | 1095 | 1 | 12 |
| β-strand | 1101 | 1 | 12 |
| α-helix | 1102 | 1 | |
| β-strand | 1103 | 1 | 13 |
| β-strand | 1107-1112 | 6 | 14 |
| α-helix | 1113-1115 | 3 | |
| β-strand | 1118-1123 | 6 | 14 |
| β-strand | 1126-1131 | 6 | 14 |
| β-strand | 1144-1148 | 5 | 14 |
| β-strand | 1157 | 1 | 13 |
| β-strand | 1159 | 1 | 11 |
| β-strand | 1163-1169 | 7 | 14 |
| β-strand | 1174-1179 | 6 | 14 |
| β-strand | 1190-1196 | 7 | 14 |
| α-helix | 1200-1206 | 7 | |
| β-strand | 1209-1215 | 7 | 14 |
| β-strand | 1220-1228 | 9 | 14 |
| β-strand | 1231-1245 | 15 | 14 |
| β-strand | 1255-1263 | 9 | 14 |
| α-helix | 1270-1272 | 3 | |
| α-helix | 1274-1276 | 3 | |
| β-strand | 1278-1282 | 5 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| D/C mosaic neurotoxin | A, B | protein | 443 | Clostridium botulinum | Q9LBR1 |
>3AZV_1 D/C mosaic neurotoxin (chains A, B) MEYFNNINEYFNSINDSKILSLQNKKNTLMDTSGYNAEVRVEGNVQLNPIFPFDFKLGSS GDDRGKVIVTQNENIVYNAMYESFSISFWIRINKWVSNLPGYTIIDSVKNNSGWSIGIIS NFLVFTLKQNENSEQDINFSYDISKNAAGYNKWFFVTITTNMMGNMMIYINGKLIDTIKV KELTGINFSKTITFQMNKIPNTGLITSDSDNINMWIRDFYIFAKELDDKDINILFNSLQY TNVVKDYWGNDLRYDKEYYMINVNYMNRYMSKKGNGIVFNTRKNNNDFNEGYKIIIKRIR GNTNDTRVRGENVLYFNTTIDNKQYSLGMYKPSRNLGTDLVPLGALDQPMDEIRKYGSFI IQPCNTFDYYASQLFLSSNATTNRLGILSIGSYSFKLGDDYWFNHEYLIPVIKIEHYASL LESTSTHWVFVPASELEHHHHHH
Structural and mutational analyses of the receptor binding domain of botulinum D/C mosaic neurotoxin: insight into the ganglioside binding mechanism. Nuemket, N., Tanaka, Y., Tsukamoto, K. et al. Biochem Biophys Res Commun (2011) 411:433-439. DOI 10.1016/j.bbrc.2011.06.173 · PubMed
Other PDB entries of the same protein (UniProt Q9LBR1), best resolution first:
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