High-resolution structure of human SHMT2 with covalently bound PLP (internal aldimine). Determined by X-ray diffraction at 1.3 Å resolution. Released 13 Aug 2025.
Explore 9RWD in 3D Show helices and sheets RCSB PDB PDBe
9RWD contains 102 α-helices and 84 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 | 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 | 166-168 | 3 | |
| α-helix | 172-174 | 3 | |
| β-strand | 177 | 1 | 4 |
| β-strand | 182 | 1 | 4 |
| α-helix | 186-189 | 4 | |
| β-strand | 191-195 | 5 | 3 |
| β-strand | 197 | 1 | 5 |
| β-strand | 204 | 1 | 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 |
| β-strand | 308 | 1 | 6 |
| α-helix | 311-317 | 7 | |
| α-helix | 318-323 | 6 | |
| α-helix | 329-342 | 14 | |
| α-helix | 345-367 | 23 | |
| β-strand | 371-372 | 2 | 7 |
| α-helix | 373-375 | 3 | |
| β-strand | 381-385 | 5 | 7 |
| α-helix | 387-389 | 3 | |
| α-helix | 393-402 | 10 | |
| β-strand | 405-406 | 2 | 1 |
| β-strand | 408-410 | 3 | 7 |
| β-strand | 423-427 | 5 | 7 |
| α-helix | 429-432 | 4 | |
| α-helix | 438-461 | 24 | |
| α-helix | 465-474 | 10 | |
| α-helix | 476-494 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 37-40 | 4 | |
| α-helix | 49-52 | 4 | |
| α-helix | 54-69 | 16 | |
| β-strand | 71-72 | 2 | 8 |
| α-helix | 82-88 | 7 | |
| α-helix | 91-94 | 4 | |
| β-strand | 99-100 | 2 | 9 |
| β-strand | 103-104 | 2 | 9 |
| α-helix | 110-126 | 17 | |
| β-strand | 134-137 | 4 | 10 |
| α-helix | 143-154 | 12 | |
| β-strand | 160-164 | 5 | 10 |
| α-helix | 166-168 | 3 | |
| α-helix | 172-174 | 3 | |
| β-strand | 177 | 1 | 11 |
| β-strand | 182 | 1 | 11 |
| α-helix | 186-189 | 4 | |
| β-strand | 191-195 | 5 | 10 |
| β-strand | 197 | 1 | 12 |
| β-strand | 204 | 1 | 12 |
| α-helix | 206-216 | 11 | |
| β-strand | 220-223 | 4 | 10 |
| α-helix | 234-244 | 11 | |
| β-strand | 247-251 | 5 | 10 |
| α-helix | 256-260 | 5 | |
| α-helix | 267-269 | 3 | |
| β-strand | 273-277 | 5 | 10 |
| α-helix | 280-282 | 3 | |
| β-strand | 288-293 | 6 | 10 |
| β-strand | 296 | 1 | 13 |
| β-strand | 308 | 1 | 13 |
| α-helix | 311-317 | 7 | |
| α-helix | 318-323 | 6 | |
| α-helix | 329-342 | 14 | |
| α-helix | 345-367 | 23 | |
| β-strand | 371-372 | 2 | 14 |
| α-helix | 373-375 | 3 | |
| β-strand | 381-385 | 5 | 14 |
| α-helix | 387-389 | 3 | |
| α-helix | 393-402 | 10 | |
| β-strand | 405-406 | 2 | 8 |
| β-strand | 408-410 | 3 | 14 |
| β-strand | 423-427 | 5 | 14 |
| α-helix | 429-432 | 4 | |
| 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 | 15 |
| α-helix | 82-88 | 7 | |
| α-helix | 91-94 | 4 | |
| β-strand | 99-100 | 2 | 16 |
| β-strand | 103-104 | 2 | 16 |
| α-helix | 110-126 | 17 | |
| β-strand | 134-137 | 4 | 17 |
| α-helix | 143-154 | 12 | |
| β-strand | 160-162 | 3 | 17 |
| β-strand | 164 | 1 | 18 |
| α-helix | 166-168 | 3 | |
| α-helix | 172-174 | 3 | |
| β-strand | 177 | 1 | 19 |
| β-strand | 182 | 1 | 19 |
| α-helix | 186-189 | 4 | |
| β-strand | 191-192 | 2 | 17 |
| β-strand | 195 | 1 | 18 |
| β-strand | 197 | 1 | 20 |
| β-strand | 204 | 1 | 20 |
| α-helix | 206-216 | 11 | |
| β-strand | 220-223 | 4 | 17 |
| α-helix | 234-244 | 11 | |
| β-strand | 247-251 | 5 | 17 |
| α-helix | 253-255 | 3 | |
| α-helix | 256-260 | 5 | |
| α-helix | 267-269 | 3 | |
| β-strand | 273-277 | 5 | 17 |
| α-helix | 280-282 | 3 | |
| β-strand | 288-293 | 6 | 17 |
| α-helix | 312-317 | 6 | |
| α-helix | 318-323 | 6 | |
| α-helix | 329-342 | 14 | |
| α-helix | 345-367 | 23 | |
| β-strand | 371-372 | 2 | 21 |
| α-helix | 373-375 | 3 | |
| β-strand | 381-385 | 5 | 21 |
| α-helix | 387-389 | 3 | |
| α-helix | 393-402 | 10 | |
| β-strand | 405-406 | 2 | 15 |
| β-strand | 408-410 | 3 | 21 |
| β-strand | 423-427 | 5 | 21 |
| α-helix | 429-432 | 4 | |
| 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 | 22 |
| α-helix | 82-88 | 7 | |
| α-helix | 91-94 | 4 | |
| β-strand | 99-100 | 2 | 23 |
| β-strand | 103-104 | 2 | 23 |
| α-helix | 110-126 | 17 | |
| β-strand | 134-137 | 4 | 24 |
| α-helix | 143-154 | 12 | |
| β-strand | 160-164 | 5 | 24 |
| α-helix | 166-168 | 3 | |
| α-helix | 172-174 | 3 | |
| β-strand | 177 | 1 | 25 |
| β-strand | 182 | 1 | 25 |
| α-helix | 186-189 | 4 | |
| β-strand | 191-195 | 5 | 24 |
| β-strand | 197 | 1 | 26 |
| β-strand | 204 | 1 | 26 |
| α-helix | 206-216 | 11 | |
| β-strand | 220-223 | 4 | 24 |
| α-helix | 234-244 | 11 | |
| β-strand | 247-251 | 5 | 24 |
| α-helix | 256-260 | 5 | |
| α-helix | 267-269 | 3 | |
| β-strand | 273-277 | 5 | 24 |
| α-helix | 280-282 | 3 | |
| β-strand | 288-293 | 6 | 24 |
| β-strand | 296 | 1 | 27 |
| β-strand | 308 | 1 | 27 |
| α-helix | 312-317 | 6 | |
| α-helix | 318-323 | 6 | |
| α-helix | 329-342 | 14 | |
| α-helix | 345-367 | 23 | |
| β-strand | 371-372 | 2 | 28 |
| α-helix | 373-375 | 3 | |
| β-strand | 381-385 | 5 | 28 |
| α-helix | 387-389 | 3 | |
| α-helix | 393-402 | 10 | |
| β-strand | 405-406 | 2 | 22 |
| β-strand | 408-410 | 3 | 28 |
| β-strand | 423-427 | 5 | 28 |
| α-helix | 429-432 | 4 | |
| α-helix | 438-461 | 24 | |
| α-helix | 465-474 | 10 | |
| α-helix | 476-494 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine hydroxymethyltransferase, mitochondrial | A, B, C, D | protein | 476 | Homo sapiens | P34897 (AlphaFold model) |
>9RWD_1 Serine hydroxymethyltransferase, mitochondrial (chains A, B, C, D) SNAAQTQTGEANRGWTGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEAL GSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPYSGSPANL AVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLIDYNQ LALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPF KHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFAVFPSLQGGPH NHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHLVLVDLRP KGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRVVDFI DEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGFDEH
High-resolution structure of human SHMT2 with covalently bound PLP (internal aldimine). Warlich, A., Ruszkowski, M., Nawrot, D. To be published.
Other PDB entries of the same protein (UniProt P34897 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9RWD directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.