Cryo-EM structure of the Human SHMT1-RNA complex. Determined by electron microscopy at 3.52 Å resolution. Released 14 Jun 2023.
Explore 8A11 in 3D Show helices and sheets RCSB PDB PDBe
8A11 contains 103 α-helices and 82 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 | 17-22 | 6 | |
| α-helix | 26-29 | 4 | |
| α-helix | 32-45 | 14 | |
| β-strand | 48 | 1 | 1 |
| α-helix | 59-65 | 7 | |
| α-helix | 68-71 | 4 | |
| α-helix | 87-103 | 17 | |
| β-strand | 111-114 | 4 | 2 |
| α-helix | 120-131 | 12 | |
| α-helix | 133 | 1 | |
| β-strand | 137-139 | 3 | 2 |
| β-strand | 141 | 1 | 3 |
| α-helix | 143-145 | 3 | |
| α-helix | 149-151 | 3 | |
| β-strand | 154 | 1 | 4 |
| β-strand | 159 | 1 | 4 |
| α-helix | 162-166 | 5 | |
| β-strand | 168-169 | 2 | 2 |
| β-strand | 172 | 1 | 3 |
| β-strand | 174 | 1 | 5 |
| β-strand | 181 | 1 | 5 |
| α-helix | 183-193 | 11 | |
| β-strand | 197-200 | 4 | 2 |
| α-helix | 211-220 | 10 | |
| β-strand | 224-228 | 5 | 2 |
| α-helix | 233-238 | 6 | |
| α-helix | 244-246 | 3 | |
| β-strand | 250-254 | 5 | 2 |
| β-strand | 265-270 | 6 | 2 |
| β-strand | 273-276 | 4 | 6 |
| β-strand | 283-285 | 3 | 6 |
| α-helix | 288-295 | 8 | |
| α-helix | 296-300 | 5 | |
| α-helix | 306-318 | 13 | |
| α-helix | 322-345 | 24 | |
| β-strand | 348-349 | 2 | 7 |
| α-helix | 350-352 | 3 | |
| β-strand | 359-362 | 4 | 7 |
| α-helix | 370-379 | 10 | |
| β-strand | 382 | 1 | 1 |
| β-strand | 385-387 | 3 | 7 |
| α-helix | 388-389 | 2 | |
| β-strand | 400-403 | 4 | 7 |
| α-helix | 406-411 | 6 | |
| α-helix | 415-439 | 25 | |
| α-helix | 445-452 | 8 | |
| α-helix | 455-472 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-22 | 8 | |
| α-helix | 26-29 | 4 | |
| α-helix | 31-46 | 16 | |
| β-strand | 48-49 | 2 | 8 |
| α-helix | 59-65 | 7 | |
| α-helix | 68-70 | 3 | |
| α-helix | 87-103 | 17 | |
| β-strand | 111 | 1 | 9 |
| β-strand | 114 | 1 | 10 |
| α-helix | 120-131 | 12 | |
| α-helix | 133 | 1 | |
| β-strand | 137-139 | 3 | 10 |
| β-strand | 141 | 1 | 11 |
| α-helix | 162-166 | 5 | |
| β-strand | 168-169 | 2 | 10 |
| β-strand | 172 | 1 | 11 |
| β-strand | 175 | 1 | 12 |
| β-strand | 180 | 1 | 12 |
| α-helix | 183-193 | 11 | |
| β-strand | 197-201 | 5 | 10 |
| α-helix | 211-221 | 11 | |
| β-strand | 224-228 | 5 | 10 |
| α-helix | 235-238 | 4 | |
| α-helix | 242-243 | 2 | |
| α-helix | 244-246 | 3 | |
| β-strand | 250-254 | 5 | 10 |
| β-strand | 265-268 | 4 | 10 |
| β-strand | 270 | 1 | 9 |
| β-strand | 273-276 | 4 | 13 |
| β-strand | 283-285 | 3 | 13 |
| α-helix | 286 | 1 | |
| α-helix | 288-296 | 9 | |
| α-helix | 306-318 | 13 | |
| α-helix | 322-344 | 23 | |
| β-strand | 349 | 1 | 14 |
| α-helix | 350-352 | 3 | |
| β-strand | 359-361 | 3 | 14 |
| α-helix | 364-366 | 3 | |
| α-helix | 372-379 | 8 | |
| β-strand | 382-383 | 2 | 8 |
| β-strand | 385 | 1 | 14 |
| β-strand | 401-403 | 3 | 14 |
| α-helix | 405-408 | 4 | |
| α-helix | 409-411 | 3 | |
| α-helix | 415-439 | 25 | |
| α-helix | 445-450 | 6 | |
| α-helix | 451-453 | 3 | |
| α-helix | 455-472 | 18 | |
| α-helix | 476-478 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-22 | 8 | |
| α-helix | 26-29 | 4 | |
| α-helix | 31-45 | 15 | |
| β-strand | 48 | 1 | 15 |
| α-helix | 56-58 | 3 | |
| α-helix | 59-65 | 7 | |
| α-helix | 68-70 | 3 | |
| α-helix | 87-103 | 17 | |
| β-strand | 111-114 | 4 | 16 |
| α-helix | 120-131 | 12 | |
| β-strand | 137-138 | 2 | 17 |
| β-strand | 139 | 1 | 16 |
| β-strand | 141 | 1 | 18 |
| α-helix | 149-151 | 3 | |
| β-strand | 154 | 1 | 19 |
| β-strand | 159 | 1 | 19 |
| α-helix | 162-166 | 5 | |
| β-strand | 168-169 | 2 | 17 |
| β-strand | 172 | 1 | 18 |
| β-strand | 174 | 1 | 20 |
| β-strand | 181 | 1 | 20 |
| α-helix | 182 | 1 | |
| α-helix | 184-193 | 10 | |
| β-strand | 197-199 | 3 | 16 |
| α-helix | 211-220 | 10 | |
| β-strand | 224-228 | 5 | 16 |
| α-helix | 234-238 | 5 | |
| β-strand | 250-254 | 5 | 16 |
| β-strand | 265-270 | 6 | 16 |
| β-strand | 273-276 | 4 | 21 |
| β-strand | 283-285 | 3 | 21 |
| α-helix | 289-294 | 6 | |
| α-helix | 295-300 | 6 | |
| α-helix | 307-318 | 12 | |
| α-helix | 322-345 | 24 | |
| β-strand | 348-349 | 2 | 22 |
| β-strand | 359-362 | 4 | 22 |
| α-helix | 370-379 | 10 | |
| β-strand | 382 | 1 | 15 |
| β-strand | 385-387 | 3 | 22 |
| α-helix | 388-389 | 2 | |
| β-strand | 400-403 | 4 | 22 |
| α-helix | 408-411 | 4 | |
| α-helix | 415-439 | 25 | |
| α-helix | 445-451 | 7 | |
| α-helix | 455-472 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-22 | 6 | |
| α-helix | 26-29 | 4 | |
| α-helix | 31-45 | 15 | |
| α-helix | 59-65 | 7 | |
| α-helix | 68-71 | 4 | |
| α-helix | 87-103 | 17 | |
| α-helix | 108-110 | 3 | |
| β-strand | 111-114 | 4 | 23 |
| α-helix | 120-131 | 12 | |
| β-strand | 138 | 1 | 24 |
| β-strand | 139 | 1 | 23 |
| β-strand | 141 | 1 | 25 |
| α-helix | 149-151 | 3 | |
| α-helix | 162-166 | 5 | |
| β-strand | 169 | 1 | 24 |
| β-strand | 172 | 1 | 25 |
| β-strand | 174 | 1 | 26 |
| α-helix | 180 | 1 | |
| β-strand | 181 | 1 | 26 |
| α-helix | 182 | 1 | |
| α-helix | 184-193 | 10 | |
| β-strand | 197-201 | 5 | 23 |
| α-helix | 211-221 | 11 | |
| β-strand | 224-228 | 5 | 23 |
| α-helix | 233-238 | 6 | |
| α-helix | 244-246 | 3 | |
| β-strand | 250-254 | 5 | 23 |
| β-strand | 265-270 | 6 | 23 |
| β-strand | 273-276 | 4 | 27 |
| β-strand | 283-285 | 3 | 27 |
| α-helix | 288-296 | 9 | |
| α-helix | 306-317 | 12 | |
| α-helix | 322-344 | 23 | |
| β-strand | 349 | 1 | 28 |
| β-strand | 358-362 | 5 | 28 |
| α-helix | 370-379 | 10 | |
| β-strand | 385-387 | 3 | 28 |
| α-helix | 388-389 | 2 | |
| β-strand | 400-404 | 5 | 28 |
| α-helix | 406-411 | 6 | |
| α-helix | 415-439 | 25 | |
| α-helix | 445-451 | 7 | |
| α-helix | 455-472 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine hydroxymethyltransferase, cytosolic | A, B, C, D | protein | 486 | Homo sapiens | P34896 (AlphaFold model) |
>8A11_1 Serine hydroxymethyltransferase, cytosolic (chains A, B, C, D) GSHMTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFA SRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQP YSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPD TGYINYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVA AGVVPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVF PGLQGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNH LILVDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKD FQKVAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPL PGLPDF
| ID | Name | Formula | Copies |
|---|---|---|---|
| PLP | Pyridoxal-5'-phosphate | C8 H10 N O6 P | 3 |
Structure-based mechanism of riboregulation of the metabolic enzyme SHMT1. Spizzichino, S., Di Fonzo, F., Marabelli, C. et al. Mol Cell (2024). DOI 10.1016/j.molcel.2024.06.016 · PubMed
Other PDB entries of the same protein (UniProt P34896 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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