Recombinant serine hydroxymethyltransferase (HUMAN). Determined by X-ray diffraction at 2.65 Å resolution. Released 16 Aug 1999.
Explore 1BJ4 in 3D Show helices and sheets RCSB PDB PDBe
1BJ4 contains 30 α-helices and 21 β-strands across 1 chain. 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 | 13-21 | 9 | |
| α-helix | 26-29 | 4 | |
| α-helix | 31-46 | 16 | |
| β-strand | 48-49 | 2 | 1 |
| α-helix | 59-65 | 7 | |
| α-helix | 68-70 | 3 | |
| β-strand | 76-77 | 2 | 2 |
| β-strand | 80-81 | 2 | 2 |
| α-helix | 87-103 | 17 | |
| β-strand | 111-114 | 4 | 3 |
| α-helix | 120-127 | 8 | |
| α-helix | 128-132 | 5 | |
| β-strand | 137-141 | 5 | 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 | 168-172 | 5 | 3 |
| β-strand | 174 | 1 | 5 |
| β-strand | 181 | 1 | 5 |
| α-helix | 183-193 | 11 | |
| β-strand | 197-200 | 4 | 3 |
| α-helix | 211-220 | 10 | |
| β-strand | 224-228 | 5 | 3 |
| α-helix | 230-232 | 3 | |
| α-helix | 233-237 | 5 | |
| α-helix | 244-246 | 3 | |
| β-strand | 250-254 | 5 | 3 |
| α-helix | 257-259 | 3 | |
| β-strand | 265-270 | 6 | 3 |
| β-strand | 273-276 | 4 | 6 |
| α-helix | 282 | 1 | |
| β-strand | 283-285 | 3 | 6 |
| α-helix | 286 | 1 | |
| α-helix | 288-294 | 7 | |
| α-helix | 295-300 | 6 | |
| α-helix | 306-318 | 13 | |
| α-helix | 322-344 | 23 | |
| α-helix | 347 | 1 | |
| β-strand | 348-349 | 2 | 7 |
| β-strand | 358-362 | 5 | 7 |
| α-helix | 363-366 | 4 | |
| α-helix | 370-379 | 10 | |
| β-strand | 382-383 | 2 | 1 |
| β-strand | 385-387 | 3 | 7 |
| β-strand | 400-404 | 5 | 7 |
| α-helix | 406-410 | 5 | |
| α-helix | 415-438 | 24 | |
| α-helix | 445-452 | 8 | |
| α-helix | 458-472 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine hydroxymethyltransferase, cytosolic | A | protein | 470 | Homo sapiens | P34896 (AlphaFold model) |
>1BJ4_1 Serine hydroxymethyltransferase, cytosolic (chains A) DADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLN NKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSGSPANFAVYTA LVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGYINYDQLEENA RLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGVVPSPFEHCHV VTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGLQGGPHNHAIA GVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLILVDLRSKGTDG GRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQKVAHFIHRGIE LTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL
| ID | Name | Formula | Copies |
|---|---|---|---|
| PLP | Pyridoxal-5'-phosphate | C8 H10 N O6 P | 1 |
The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy. Renwick, S.B., Snell, K., Baumann, U. Structure (1998) 6:1105-1116. DOI 10.1016/S0969-2126(98)00112-9 · 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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