Crystal structure of clostridium neurotoxin type B. Determined by X-ray diffraction at 1.9 Å resolution. Released 1 Nov 2000.
Explore 1EPW in 3D Show helices and sheets RCSB PDB PDBe
1EPW contains 63 α-helices and 88 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 | 12-13 | 2 | |
| β-strand | 18-22 | 5 | 1 |
| α-helix | 24-26 | 3 | |
| β-strand | 33-39 | 7 | 1 |
| β-strand | 42-45 | 4 | 1 |
| α-helix | 55-58 | 4 | |
| β-strand | 63-64 | 2 | 2 |
| β-strand | 71-72 | 2 | 3 |
| β-strand | 73 | 1 | 4 |
| α-helix | 81-98 | 18 | |
| α-helix | 102-113 | 12 | |
| α-helix | 115-117 | 3 | |
| β-strand | 127-128 | 2 | 5 |
| β-strand | 136-140 | 5 | 1 |
| α-helix | 143 | 1 | |
| β-strand | 150-154 | 5 | 1 |
| β-strand | 157-160 | 4 | 1 |
| β-strand | 165 | 1 | 4 |
| β-strand | 170-172 | 3 | 1 |
| β-strand | 175-176 | 2 | 6 |
| β-strand | 179-180 | 2 | 6 |
| α-helix | 181-183 | 3 | |
| β-strand | 190-193 | 4 | 1 |
| β-strand | 198-202 | 5 | 7 |
| β-strand | 219-220 | 2 | 7 |
| α-helix | 223-238 | 16 | |
| α-helix | 247 | 1 | |
| β-strand | 248 | 1 | 8 |
| β-strand | 250 | 1 | 9 |
| β-strand | 257 | 1 | 10 |
| α-helix | 258-259 | 2 | |
| β-strand | 263 | 1 | 8 |
| α-helix | 265-271 | 7 | |
| α-helix | 275-278 | 4 | |
| α-helix | 281-304 | 24 | |
| β-strand | 307-308 | 2 | 5 |
| α-helix | 316-326 | 11 | |
| β-strand | 330-331 | 2 | 11 |
| β-strand | 337-338 | 2 | 11 |
| α-helix | 341-349 | 9 | |
| α-helix | 350-354 | 5 | |
| α-helix | 357-364 | 8 | |
| β-strand | 377-382 | 6 | 7 |
| β-strand | 392 | 1 | 12 |
| β-strand | 396 | 1 | 12 |
| α-helix | 400-402 | 3 | |
| α-helix | 406-411 | 6 | |
| β-strand | 412 | 1 | 7 |
| α-helix | 417-419 | 3 | |
| β-strand | 420-421 | 2 | 7 |
| α-helix | 422-424 | 3 | |
| α-helix | 425-427 | 3 | |
| β-strand | 428-429 | 2 | 3 |
| β-strand | 432-436 | 5 | 13 |
| β-strand | 445-449 | 5 | 13 |
| α-helix | 450-452 | 3 | |
| β-strand | 454 | 1 | 10 |
| α-helix | 455 | 1 | |
| β-strand | 457 | 1 | 9 |
| α-helix | 459-461 | 3 | |
| α-helix | 465-467 | 3 | |
| β-strand | 470-472 | 3 | 14 |
| α-helix | 487-492 | 6 | |
| α-helix | 502-504 | 3 | |
| β-strand | 506-507 | 2 | 1 |
| α-helix | 508-510 | 3 | |
| β-strand | 516 | 1 | 6 |
| β-strand | 523-524 | 2 | 2 |
| β-strand | 526-530 | 5 | 13 |
| α-helix | 536-541 | 6 | |
| β-strand | 553-555 | 3 | 15 |
| α-helix | 558-563 | 6 | |
| β-strand | 567-569 | 3 | 15 |
| α-helix | 574-580 | 7 | |
| α-helix | 586-605 | 20 | |
| α-helix | 606-608 | 3 | |
| β-strand | 611 | 1 | 16 |
| α-helix | 612-614 | 3 | |
| β-strand | 616 | 1 | 16 |
| α-helix | 623-627 | 5 | |
| α-helix | 638-645 | 8 | |
| α-helix | 646-650 | 5 | |
| α-helix | 662-664 | 3 | |
| β-strand | 665-667 | 3 | 14 |
| α-helix | 668-669 | 2 | |
| α-helix | 674-702 | 29 | |
| α-helix | 703-707 | 5 | |
| α-helix | 708-737 | 30 | |
| α-helix | 742-746 | 5 | |
| α-helix | 752-781 | 30 | |
| α-helix | 782-786 | 5 | |
| α-helix | 787-811 | 25 | |
| α-helix | 813-816 | 4 | |
| α-helix | 824-830 | 7 | |
| α-helix | 834-837 | 4 | |
| α-helix | 839-841 | 3 | |
| α-helix | 846-856 | 11 | |
| α-helix | 859-862 | 4 | |
| β-strand | 863-866 | 4 | 17 |
| β-strand | 867-869 | 3 | 18 |
| β-strand | 874-876 | 3 | 18 |
| β-strand | 883-886 | 4 | 19 |
| β-strand | 891-892 | 2 | 17 |
| β-strand | 897-900 | 4 | 17 |
| β-strand | 908-911 | 4 | 19 |
| β-strand | 925-932 | 8 | 17 |
| α-helix | 933-937 | 5 | |
| α-helix | 938-940 | 3 | |
| α-helix | 941-946 | 6 | |
| β-strand | 948-956 | 9 | 19 |
| β-strand | 959-966 | 8 | 19 |
| β-strand | 969-975 | 7 | 19 |
| β-strand | 981-987 | 7 | 19 |
| β-strand | 1002-1008 | 7 | 17 |
| β-strand | 1012-1017 | 6 | 17 |
| β-strand | 1020-1026 | 7 | 17 |
| β-strand | 1038-1045 | 8 | 19 |
| β-strand | 1053-1061 | 9 | 17 |
| α-helix | 1064-1066 | 3 | |
| α-helix | 1067-1078 | 12 | |
| β-strand | 1082 | 1 | 20 |
| β-strand | 1084 | 1 | 21 |
| β-strand | 1090 | 1 | 21 |
| α-helix | 1091 | 1 | |
| β-strand | 1092-1093 | 2 | 22 |
| β-strand | 1096-1097 | 2 | 23 |
| β-strand | 1098-1101 | 4 | 24 |
| β-strand | 1107-1111 | 5 | 23 |
| β-strand | 1118-1122 | 5 | 23 |
| α-helix | 1123-1124 | 2 | |
| β-strand | 1125 | 1 | 25 |
| β-strand | 1136 | 1 | 25 |
| β-strand | 1144-1148 | 5 | 23 |
| β-strand | 1158-1159 | 2 | 22 |
| β-strand | 1161 | 1 | 20 |
| β-strand | 1165-1172 | 8 | 23 |
| β-strand | 1175-1180 | 6 | 23 |
| β-strand | 1181-1182 | 2 | 26 |
| β-strand | 1189-1191 | 3 | 23 |
| α-helix | 1192 | 1 | |
| β-strand | 1193-1196 | 4 | 23 |
| β-strand | 1203-1204 | 2 | 26 |
| β-strand | 1207-1210 | 4 | 23 |
| β-strand | 1220 | 1 | 24 |
| β-strand | 1221-1225 | 5 | 23 |
| β-strand | 1233-1245 | 13 | 23 |
| β-strand | 1250-1259 | 10 | 23 |
| α-helix | 1261-1265 | 5 | |
| β-strand | 1279-1282 | 4 | 24 |
| β-strand | 1285 | 1 | 27 |
| β-strand | 1288 | 1 | 27 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Botulinum neurotoxin type B | A | protein | 1290 | Clostridium botulinum | P10844 (AlphaFold model) |
>1EPW_1 BOTULINUM NEUROTOXIN TYPE B (chains A) PVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITDRIWIIPERYTFGYKPEDFNK SSGIFNRDVCEYYDPDYLNTNDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGD RRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIFGPGPVLNENETIDIGIQNHF ASREGFGGIMQMKFCPEYVSVFNNVQENKGASIFNRRGYFSDPALILMHELIHVLHGLYG IKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIITPSTDKSIYDKVLQNFRGIVD RLNKVLVCISDPNININIYKNKFKDKYKFVEDSEGKYSIDVESFDKLYKSLMFGFTETNI AENYKIKTRASYFSDSLPPVKIKNLLDNEIYTIEEGFNISDKDMEKEYRGQNKAINKQAY EEISKEHLAVYKIQMCKSVKAPGICIDVDNEDLFFIADKNSFSDDLSKNERIEYNTQSNY IENDFPINELILDTDLISKIELPSENTESLTDFNVDVPVYEKQPAIKKIFTDENTIFQYL YSQTFPLDIRDISLTSSFDDALLFSNKVYSFFSMDYIKTANKVVEAGLFAGWVKQIVNDF VIEANKSNTMDKIADISLIVPYIGLALNVGNETAKGNFENAFEIAGASILLEFIPELLIP VVGAFLLESYIDNKNKIIKTIDNALTKRNEKWSDMYGLIVAQWLSTVNTQFYTIKEGMYK ALNYQAQALEEIIKYRYNIYSEKEKSNINIDFNDINSKLNEGINQAIDNINNFINGCSVS YLMKKMIPLAVEKLLDFDNTLKKNLLNYIDENKLYLIGSAEYEKSKVNKYLKTIMPFDLS IYTNDTILIEMFNKYNSEILNNIILNLRYKDNNLIDLSGYGAKVEVYDGVELNDKNQFKL TSSANSKIRVTQNQNIIFNSVFLDFSVSFWIRIPKYKNDGIQNYIHNEYTIINCMKNNSG WKISIRGNRIIWTLIDINGKTKSVFFEYNIREDISEYINRWFFVTITNNLNNAKIYINGK LESNTDIKDIREVIANGEIIFKLDGDIDRTQFIWMKYFSIFNTELSQSNIEERYKIQSYS EYLKDFWGNPLMYNKEYYMFNAGNKNSYIKLKKDSPVGEILTRSKYNQNSKYINYRDLYI GEKFIIRRKSNSQSINDDIVRKEDYIYLDFFNLNQEWRVYTYKYFKKEEEKLFLAPISDS DEFYNTIQIKEYDEQPTYSCQLLFKKDEESTDEIGLIGIHRFYESGIVFEEYKDYFCISK WYLKEVKRKPYNLKLGCNWQFIPKDEGWTE
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Water and common crystallization additives (SO4) are not listed.
Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Swaminathan, S., Eswaramoorthy, S. Nat Struct Biol (2000) 7:693-699. DOI 10.1038/78005 · PubMed
Other PDB entries of the same protein (UniProt P10844 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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