Room-temperature X-ray structure of human mitochondrial serine hydroxymethyltransferase (hSHMT2). Determined by X-ray diffraction at 2.5 Å resolution. Released 16 Aug 2023.
Explore 8SSJ in 3D Show helices and sheets RCSB PDB PDBe
8SSJ contains 50 α-helices and 44 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 | 49-52 | 4 | |
| α-helix | 54-69 | 16 | |
| β-strand | 71-72 | 2 | 1 |
| α-helix | 82-88 | 7 | |
| α-helix | 91-94 | 4 | |
| β-strand | 99-100 | 2 | 2 |
| β-strand | 103-104 | 2 | 2 |
| α-helix | 110-126 | 17 | |
| β-strand | 134-137 | 4 | 3 |
| α-helix | 143-154 | 12 | |
| β-strand | 160-164 | 5 | 3 |
| α-helix | 172-174 | 3 | |
| β-strand | 177 | 1 | 4 |
| β-strand | 182 | 1 | 4 |
| α-helix | 185-187 | 3 | |
| β-strand | 191-195 | 5 | 3 |
| β-strand | 197-198 | 2 | 5 |
| β-strand | 203-204 | 2 | 5 |
| α-helix | 206-216 | 11 | |
| β-strand | 220-223 | 4 | 3 |
| α-helix | 234-244 | 11 | |
| β-strand | 247-251 | 5 | 3 |
| α-helix | 256-260 | 5 | |
| α-helix | 267-269 | 3 | |
| β-strand | 273-277 | 5 | 3 |
| α-helix | 280-282 | 3 | |
| β-strand | 288-293 | 6 | 3 |
| β-strand | 296 | 1 | 6 |
| α-helix | 307 | 1 | |
| β-strand | 308 | 1 | 6 |
| α-helix | 309 | 1 | |
| α-helix | 312-317 | 6 | |
| α-helix | 318-323 | 6 | |
| α-helix | 329-341 | 13 | |
| α-helix | 345-367 | 23 | |
| β-strand | 371-372 | 2 | 7 |
| α-helix | 373-375 | 3 | |
| β-strand | 381-385 | 5 | 7 |
| α-helix | 393-401 | 9 | |
| β-strand | 405-406 | 2 | 1 |
| β-strand | 408-410 | 3 | 7 |
| β-strand | 413 | 1 | 8 |
| β-strand | 415 | 1 | 8 |
| β-strand | 423-427 | 5 | 7 |
| α-helix | 429-433 | 5 | |
| α-helix | 438-461 | 24 | |
| α-helix | 465-474 | 10 | |
| α-helix | 476-494 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 49-52 | 4 | |
| α-helix | 54-69 | 16 | |
| β-strand | 71-72 | 2 | 9 |
| α-helix | 82-88 | 7 | |
| α-helix | 91-94 | 4 | |
| β-strand | 99-100 | 2 | 10 |
| β-strand | 103-104 | 2 | 10 |
| α-helix | 110-126 | 17 | |
| β-strand | 134-137 | 4 | 11 |
| α-helix | 143-154 | 12 | |
| β-strand | 160-164 | 5 | 11 |
| α-helix | 166-168 | 3 | |
| α-helix | 172-174 | 3 | |
| β-strand | 177 | 1 | 12 |
| β-strand | 182 | 1 | 12 |
| α-helix | 185-187 | 3 | |
| β-strand | 191-195 | 5 | 11 |
| β-strand | 197 | 1 | 13 |
| β-strand | 204 | 1 | 13 |
| α-helix | 206-216 | 11 | |
| β-strand | 220-223 | 4 | 11 |
| α-helix | 234-244 | 11 | |
| β-strand | 247-251 | 5 | 11 |
| α-helix | 256-260 | 5 | |
| α-helix | 267-269 | 3 | |
| β-strand | 273-277 | 5 | 11 |
| α-helix | 280-282 | 3 | |
| β-strand | 288-293 | 6 | 11 |
| β-strand | 296 | 1 | 14 |
| β-strand | 308 | 1 | 14 |
| α-helix | 311-317 | 7 | |
| α-helix | 318-323 | 6 | |
| α-helix | 329-341 | 13 | |
| α-helix | 345-366 | 22 | |
| β-strand | 371-372 | 2 | 15 |
| α-helix | 373-375 | 3 | |
| β-strand | 381-385 | 5 | 15 |
| α-helix | 387-389 | 3 | |
| α-helix | 393-401 | 9 | |
| β-strand | 405-406 | 2 | 9 |
| β-strand | 408-410 | 3 | 15 |
| β-strand | 423-427 | 5 | 15 |
| α-helix | 429-433 | 5 | |
| α-helix | 438-459 | 22 | |
| α-helix | 465-474 | 10 | |
| α-helix | 476-494 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine hydroxymethyltransferase, mitochondrial | A, B | protein | 468 | Homo sapiens | P34897 (AlphaFold model) |
>8SSJ_1 Serine hydroxymethyltransferase, mitochondrial (chains A, B) GEANRGWTGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKY SEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQ PHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLIDYNQLALTARLF RPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTT TTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVA VALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARA ERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGL EVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGFDEH
Revealing protonation states and tracking substrate in serine hydroxymethyltransferase with room-temperature X-ray and neutron crystallography. Drago, V.N., Campos, C., Hooper, M. et al. Commun Chem (2023) 6:162-162. DOI 10.1038/s42004-023-00964-9 · PubMed
Other PDB entries of the same protein (UniProt P34897 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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