Crystal structure of mouse Xyloside xylosyltransferase 1 complexed with manganese. Determined by X-ray diffraction at 3.0 Å resolution. Released 30 Sept 2015.
Explore 4WLM in 3D Show helices and sheets RCSB PDB PDBe
4WLM contains 45 α-helices and 24 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 |
|---|---|---|---|
| β-strand | 97-103 | 7 | 1 |
| α-helix | 111-126 | 16 | |
| β-strand | 135-142 | 8 | 1 |
| α-helix | 144-154 | 11 | |
| β-strand | 165-172 | 8 | 1 |
| α-helix | 173-184 | 12 | |
| α-helix | 185-187 | 3 | |
| α-helix | 200-209 | 10 | |
| α-helix | 210-213 | 4 | |
| β-strand | 221-224 | 4 | 1 |
| β-strand | 228-230 | 3 | 2 |
| α-helix | 235-238 | 4 | |
| α-helix | 239-243 | 5 | |
| α-helix | 244-245 | 2 | |
| β-strand | 250-254 | 5 | 1 |
| α-helix | 255 | 1 | |
| α-helix | 259-263 | 5 | |
| α-helix | 265-270 | 6 | |
| β-strand | 276 | 1 | 3 |
| α-helix | 278-279 | 2 | |
| β-strand | 284 | 1 | 3 |
| β-strand | 287-294 | 8 | 1 |
| α-helix | 296-301 | 6 | |
| α-helix | 303-308 | 6 | |
| α-helix | 311-321 | 11 | |
| α-helix | 329-339 | 11 | |
| α-helix | 341-343 | 3 | |
| β-strand | 344-347 | 4 | 1 |
| α-helix | 349-351 | 3 | |
| β-strand | 353-354 | 2 | 2 |
| α-helix | 358-360 | 3 | |
| α-helix | 368-372 | 5 | |
| β-strand | 380-382 | 3 | 2 |
| α-helix | 384-386 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 97-103 | 7 | 4 |
| α-helix | 111-127 | 17 | |
| β-strand | 135-141 | 7 | 4 |
| α-helix | 144-156 | 13 | |
| β-strand | 165-171 | 7 | 4 |
| α-helix | 173-184 | 12 | |
| α-helix | 188-190 | 3 | |
| α-helix | 195-197 | 3 | |
| α-helix | 200-205 | 6 | |
| α-helix | 210-212 | 3 | |
| β-strand | 220-224 | 5 | 4 |
| β-strand | 228-230 | 3 | 5 |
| α-helix | 235-238 | 4 | |
| α-helix | 239-243 | 5 | |
| α-helix | 244-245 | 2 | |
| β-strand | 250-254 | 5 | 4 |
| α-helix | 255 | 1 | |
| α-helix | 259-263 | 5 | |
| α-helix | 265-270 | 6 | |
| β-strand | 276 | 1 | 6 |
| α-helix | 278-279 | 2 | |
| β-strand | 284 | 1 | 6 |
| β-strand | 287-295 | 9 | 4 |
| α-helix | 296-301 | 6 | |
| α-helix | 303-307 | 5 | |
| α-helix | 311-321 | 11 | |
| α-helix | 329-339 | 11 | |
| α-helix | 341-343 | 3 | |
| β-strand | 344-347 | 4 | 4 |
| α-helix | 349-351 | 3 | |
| β-strand | 353-354 | 2 | 5 |
| α-helix | 358-362 | 5 | |
| α-helix | 368-372 | 5 | |
| β-strand | 380-382 | 3 | 5 |
| α-helix | 384-386 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Xyloside xylosyltransferase 1 | A, B | protein | 306 | Mus musculus | Q3U4G3 (AlphaFold model) |
>4WLM_1 Xyloside xylosyltransferase 1 (chains A, B) SLEGGVVVPVDYHLLMMFTKAEHNAPLQAKARVALSSLLRLAKFEAHEVLNLHFVSEEAS REVAKALLRELLPPAAGFKCKVIFHDVAVLTDKLFPVVEAMQKYFSAGSGTYYSDSIFFL SVAMHQIMPKEIPRIIQLDLDLKYKTNIRELFEEFDNFLPGAVIGIAREMQPVYRHTFWQ FRHENPKTRVGDPPPEGLPGFNSGVMLLNLEAMRQSPLYSHLLEPSWVQQLADKYHFRGH LGDQDFFTMIGMEHPELFHVLDCTWNRQLCTWWRDHGYSDVFQAYFRCEGHVKIYHGNCN TPIPED
| ID | Name | Formula | Copies |
|---|---|---|---|
| MN | Manganese (II) ion | Mn | 2 |
Water and common crystallization additives (SO4) are not listed.
Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism. Yu, H., Takeuchi, M., LeBarron, J. et al. Nat Chem Biol (2015) 11:847-854. DOI 10.1038/nchembio.1927 · PubMed
Other PDB entries of the same protein (UniProt Q3U4G3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4WLM 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.