Structures of TcdB in complex with R-Ras. Determined by X-ray diffraction at 2.34 Å resolution. Released 8 Sept 2021.
Explore 7S0Z in 3D Show helices and sheets RCSB PDB PDBe
7S0Z contains 85 α-helices and 42 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 |
|---|---|---|---|
| α-helix | 6-12 | 7 | |
| α-helix | 22-34 | 13 | |
| α-helix | 42-62 | 21 | |
| α-helix | 69-89 | 21 | |
| β-strand | 92-93 | 2 | 5 |
| α-helix | 94-95 | 2 | |
| β-strand | 97-101 | 5 | 6 |
| α-helix | 109-121 | 13 | |
| β-strand | 126-131 | 6 | 6 |
| α-helix | 138-155 | 18 | |
| α-helix | 168-196 | 29 | |
| α-helix | 202-214 | 13 | |
| α-helix | 218-233 | 16 | |
| β-strand | 237-239 | 3 | 6 |
| α-helix | 240-242 | 3 | |
| α-helix | 244-247 | 4 | |
| α-helix | 252-256 | 5 | |
| α-helix | 257-262 | 6 | |
| α-helix | 265-279 | 15 | |
| β-strand | 282-285 | 4 | 6 |
| β-strand | 290 | 1 | 7 |
| α-helix | 291-292 | 2 | |
| β-strand | 293 | 1 | 8 |
| α-helix | 294 | 1 | |
| α-helix | 302-304 | 3 | |
| α-helix | 310-325 | 16 | |
| α-helix | 336-338 | 3 | |
| α-helix | 341-352 | 12 | |
| α-helix | 357-359 | 3 | |
| β-strand | 361 | 1 | 8 |
| α-helix | 362-363 | 2 | |
| β-strand | 368-369 | 2 | 5 |
| β-strand | 375-379 | 5 | 6 |
| β-strand | 382-390 | 9 | 6 |
| α-helix | 395-419 | 25 | |
| α-helix | 425-439 | 15 | |
| α-helix | 445-451 | 7 | |
| α-helix | 454-456 | 3 | |
| α-helix | 465-469 | 5 | |
| α-helix | 472-484 | 13 | |
| α-helix | 496-499 | 4 | |
| α-helix | 500-502 | 3 | |
| β-strand | 503 | 1 | 6 |
| α-helix | 506-508 | 3 | |
| β-strand | 510 | 1 | 7 |
| α-helix | 525-539 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-12 | 7 | |
| α-helix | 22-34 | 13 | |
| α-helix | 42-62 | 21 | |
| α-helix | 69-89 | 21 | |
| β-strand | 92-93 | 2 | 1 |
| α-helix | 94-95 | 2 | |
| β-strand | 97-101 | 5 | 2 |
| α-helix | 106-108 | 3 | |
| α-helix | 109-121 | 13 | |
| β-strand | 126-131 | 6 | 2 |
| α-helix | 138-155 | 18 | |
| α-helix | 168-196 | 29 | |
| α-helix | 202-214 | 13 | |
| α-helix | 218-233 | 16 | |
| β-strand | 237-239 | 3 | 2 |
| α-helix | 240-242 | 3 | |
| α-helix | 244-247 | 4 | |
| α-helix | 252-256 | 5 | |
| α-helix | 257-261 | 5 | |
| α-helix | 265-279 | 15 | |
| β-strand | 282-285 | 4 | 2 |
| β-strand | 290 | 1 | 3 |
| α-helix | 291-292 | 2 | |
| β-strand | 293 | 1 | 4 |
| α-helix | 294 | 1 | |
| α-helix | 302-304 | 3 | |
| α-helix | 310-325 | 16 | |
| α-helix | 336-338 | 3 | |
| α-helix | 341-352 | 12 | |
| α-helix | 357-359 | 3 | |
| β-strand | 361 | 1 | 4 |
| α-helix | 362-363 | 2 | |
| β-strand | 368-369 | 2 | 1 |
| β-strand | 375-379 | 5 | 2 |
| β-strand | 382-390 | 9 | 2 |
| α-helix | 395-419 | 25 | |
| α-helix | 425-439 | 15 | |
| α-helix | 445-450 | 6 | |
| α-helix | 454-456 | 3 | |
| α-helix | 465-469 | 5 | |
| α-helix | 472-483 | 12 | |
| α-helix | 496-499 | 4 | |
| α-helix | 500-502 | 3 | |
| β-strand | 503 | 1 | 2 |
| α-helix | 504-505 | 2 | |
| α-helix | 506-508 | 3 | |
| β-strand | 510 | 1 | 3 |
| α-helix | 515-517 | 3 | |
| α-helix | 525-540 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 24-27 | 4 | |
| β-strand | 28-35 | 8 | 9 |
| α-helix | 42-51 | 10 | |
| β-strand | 66-72 | 7 | 9 |
| β-strand | 75-83 | 9 | 9 |
| α-helix | 91-99 | 9 | |
| β-strand | 103-109 | 7 | 9 |
| α-helix | 113-130 | 18 | |
| β-strand | 137-142 | 6 | 9 |
| α-helix | 147-149 | 3 | |
| α-helix | 154-163 | 10 | |
| β-strand | 168-170 | 3 | 9 |
| β-strand | 172 | 1 | 10 |
| β-strand | 177 | 1 | 10 |
| α-helix | 179-196 | 18 | |
| α-helix | 200 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 24-27 | 4 | |
| β-strand | 28-35 | 8 | 11 |
| α-helix | 42-51 | 10 | |
| β-strand | 67-72 | 6 | 11 |
| β-strand | 75-83 | 9 | 11 |
| α-helix | 91-99 | 9 | |
| β-strand | 103-109 | 7 | 11 |
| α-helix | 113-130 | 18 | |
| β-strand | 137-142 | 6 | 11 |
| α-helix | 144-149 | 6 | |
| α-helix | 154-163 | 10 | |
| β-strand | 168-170 | 3 | 11 |
| β-strand | 172 | 1 | 12 |
| β-strand | 177 | 1 | 12 |
| α-helix | 179-196 | 18 | |
| α-helix | 200 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Toxin B | A, B | protein | 541 | Clostridioides difficile | Q9EXR0 (AlphaFold model) |
| Ras-related protein R-Ras | C, D | protein | 179 | Homo sapiens | P10301 (AlphaFold model) |
>7S0Z_1 Toxin B (chains A, B) MSLVNRKQLEKMANVRFRVQEDEYVAILDALEEYHNMSENTVVEKYLKLKDINSLTDTYI DTYKKSGRNKALKKFKEYLVIEILELKNSNLTPVEKNLHFIWIGGQINDTAINYINQWKD VNSDYNVNVFYDSNAFLINTLKKTIIESASNDTLESFRENLNDPEFNHTAFFRKRMQIIY DKQQNFINYYKAQKEENPDLIIDDIVKTYLSNEYSKDIDELNAYIEESLNKVTENSGNDV RNFEEFKTGEVFNLYEQELVERWNLAGASDILRVAILKNIGGVYLDVDMLPGIHPDLFKD INKPDSVKTAVDWEEMQLEAIMKHKEYIPEYTSKHFDTLDEEVQSSFESVLASKSDKSEI FLPLGDIEVSPLEVKIAFAKGSIINQALISAKDSYCSDLLIKQIQNRYKILNDTLGPIIS QGNDFNTTMNNFGESLGAIANEENISFIAKIGSYLRVGFYPEANTTITLSGPTIYAGAYK DLLTFKEMSIDTSILSSELRNFEFPKVNISQATEQEKNSLWQFNEERAKIQFEEYKKNYF E
>7S0Z_2 Ras-related protein R-Ras (chains C, D) DPPPSETHKLVVVGGGGVGKSALTIQFIQSYFVSDYDPNIEDSYTKICSVDGIPARLDIL DTAGQEEFGAMREQYMRAGHGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPVVLVGN KADLESQRQVPRSEASAFGASHHVAYFEASAKLRLNVDEAFEQLVRAVRKYQEQELPPS
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 5 |
| GLC | alpha-D-glucopyranose | C6 H12 O6 | 2 |
| MN | Manganese (II) ion | Mn | 2 |
| UDP | Uridine-5'-diphosphate | C9 H14 N2 O12 P2 | 2 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 2 |
Water and common crystallization additives (PEG, ACT, EDO, NH4) are not listed.
Structural basis for selective modification of Rho and Ras GTPases by Clostridioides difficile toxin B. Liu, Z., Zhang, S., Chen, P. et al. Sci Adv (2021) 7:eabi4582-eabi4582. DOI 10.1126/sciadv.abi4582 · PubMed
Other PDB entries of the same protein (UniProt Q9EXR0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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