Structure of SHMT2 in complex with CBX. Determined by X-ray diffraction at 2.76 Å resolution. Released 15 Sept 2021.
Explore 7BYI in 3D Show helices and sheets RCSB PDB PDBe
7BYI contains 48 α-helices and 41 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 | |
| α-helix | 110-126 | 17 | |
| β-strand | 134-137 | 4 | 2 |
| α-helix | 143-154 | 12 | |
| β-strand | 160-163 | 4 | 2 |
| α-helix | 172-174 | 3 | |
| β-strand | 177 | 1 | 3 |
| β-strand | 182 | 1 | 3 |
| α-helix | 186-189 | 4 | |
| β-strand | 191-194 | 4 | 2 |
| β-strand | 197-198 | 2 | 4 |
| β-strand | 203-204 | 2 | 4 |
| α-helix | 206-215 | 10 | |
| β-strand | 220-223 | 4 | 2 |
| α-helix | 237-244 | 8 | |
| β-strand | 247-251 | 5 | 2 |
| α-helix | 256-261 | 6 | |
| α-helix | 267-269 | 3 | |
| β-strand | 273-277 | 5 | 2 |
| β-strand | 288-293 | 6 | 2 |
| β-strand | 296-298 | 3 | 5 |
| α-helix | 306 | 1 | |
| β-strand | 307-308 | 2 | 5 |
| α-helix | 309 | 1 | |
| α-helix | 311-317 | 7 | |
| α-helix | 318-323 | 6 | |
| α-helix | 329-342 | 14 | |
| α-helix | 345-367 | 23 | |
| β-strand | 372 | 1 | 6 |
| β-strand | 375 | 1 | 6 |
| β-strand | 381-385 | 5 | 6 |
| α-helix | 393-401 | 9 | |
| β-strand | 405-406 | 2 | 1 |
| β-strand | 408-410 | 3 | 6 |
| β-strand | 423-427 | 5 | 6 |
| α-helix | 429-432 | 4 | |
| α-helix | 438-459 | 22 | |
| α-helix | 466-474 | 9 | |
| α-helix | 476-494 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 49-52 | 4 | |
| α-helix | 54-69 | 16 | |
| β-strand | 71-72 | 2 | 7 |
| α-helix | 82-88 | 7 | |
| α-helix | 91-94 | 4 | |
| β-strand | 99-100 | 2 | 8 |
| β-strand | 103-104 | 2 | 8 |
| α-helix | 110-127 | 18 | |
| β-strand | 134-137 | 4 | 9 |
| α-helix | 143-154 | 12 | |
| β-strand | 160-163 | 4 | 9 |
| α-helix | 172-174 | 3 | |
| β-strand | 177 | 1 | 10 |
| β-strand | 182 | 1 | 10 |
| α-helix | 186-189 | 4 | |
| β-strand | 191-192 | 2 | 9 |
| β-strand | 197 | 1 | 11 |
| β-strand | 204 | 1 | 11 |
| α-helix | 206-215 | 10 | |
| β-strand | 220-224 | 5 | 9 |
| α-helix | 234-244 | 11 | |
| α-helix | 246 | 1 | |
| β-strand | 247-251 | 5 | 9 |
| α-helix | 256-261 | 6 | |
| α-helix | 265-266 | 2 | |
| α-helix | 267-269 | 3 | |
| β-strand | 273-277 | 5 | 9 |
| α-helix | 280-282 | 3 | |
| β-strand | 288-293 | 6 | 9 |
| β-strand | 296 | 1 | 12 |
| β-strand | 308 | 1 | 12 |
| α-helix | 311-317 | 7 | |
| α-helix | 318-323 | 6 | |
| α-helix | 329-340 | 12 | |
| α-helix | 345-364 | 20 | |
| α-helix | 365-369 | 5 | |
| β-strand | 371-373 | 3 | 13 |
| β-strand | 381-385 | 5 | 13 |
| α-helix | 393-401 | 9 | |
| β-strand | 405-406 | 2 | 7 |
| β-strand | 408-410 | 3 | 13 |
| β-strand | 423-427 | 5 | 13 |
| α-helix | 429-432 | 4 | |
| α-helix | 440-459 | 20 | |
| α-helix | 465-474 | 10 | |
| α-helix | 476-494 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine hydroxymethyltransferase, mitochondrial | A | protein | 483 | Homo sapiens | P34897 (AlphaFold model) |
| Serine hydroxymethyltransferase, mitochondrial | B | protein | 483 | Homo sapiens | P34897 (AlphaFold model) |
>7BYI_1 Serine hydroxymethyltransferase, mitochondrial (chains A) MAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCS RAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPY SGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKT GLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAG KVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFAVFP SLQGGPHNHAIAAVAVALKQAATPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHL VLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDF RRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGF DEH
>7BYI_2 Serine hydroxymethyltransferase, mitochondrial (chains B) MAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCS RAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPY SGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYGLAPKT GLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAA KVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREAPYTFEDRINFAVFP SLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGGYLVSGGTDNHL VLVDLRPKGGGGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDF RRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGF DEH
Water and common crystallization additives (PEG) are not listed.
Structure of SHMT2 with CBX. Li, L., Su, D. To be published.
Other PDB entries of the same protein (UniProt P34897 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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