4WLG: Mouse Xyloside xylosyltransferase 1, apo form

crystal structure of mouse Xyloside xylosyltransferase 1, apo form. Determined by X-ray diffraction at 3.0 Å resolution. Released 4 Nov 2015.

Method
X-ray diffraction
Resolution
3.0 Å
Organism
Mus musculus
Chains
2
Atoms
4,772
Mol. weight
71.07 kDa
Released
4 Nov 2015

Explore 4WLG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4WLG contains 44 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.

Chain A: 22 helices, 12 β-strands

ElementResiduesLengthSheet
β-strand97-10371
α-helix111-12515
β-strand135-14171
α-helix144-15714
β-strand166-17161
α-helix173-18412
α-helix185-1873
α-helix200-2056
α-helix207-2093
α-helix210-2134
β-strand221-22441
β-strand228-23032
α-helix234-2363
α-helix238-2436
α-helix244-2452
β-strand250-25451
α-helix2551
α-helix259-2635
α-helix265-2706
β-strand27613
α-helix278-2792
β-strand28413
β-strand287-29481
α-helix296-3016
α-helix303-3086
α-helix311-32111
α-helix329-33911
α-helix341-3433
β-strand344-34741
α-helix349-3513
β-strand353-35422
α-helix358-3603
α-helix368-3725
β-strand380-38232
Chain B: 22 helices, 12 β-strands
ElementResiduesLengthSheet
β-strand97-10374
α-helix111-12515
β-strand135-14174
α-helix144-15613
β-strand165-17174
α-helix173-18412
α-helix188-1914
α-helix195-1973
α-helix200-2056
α-helix210-2123
β-strand220-22454
β-strand228-23035
α-helix235-2384
α-helix239-2435
α-helix244-2452
β-strand250-25454
α-helix2551
α-helix259-2635
α-helix265-2706
β-strand27616
α-helix278-2792
β-strand28416
β-strand287-29594
α-helix296-3016
α-helix307-3093
α-helix311-32111
α-helix329-33911
α-helix341-3433
β-strand344-34744
α-helix349-3524
β-strand353-35425
α-helix358-3625
α-helix368-3725
β-strand380-38235

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Xyloside xylosyltransferase 1A, Bprotein306Mus musculusQ3U4G3 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4WLG_1 Xyloside xylosyltransferase 1 (chains A, B)
SLEGGVVVPVDYHLLMMFTKAEHNAPLQAKARVALSSLLRLAKFEAHEVLNLHFVSEEAS
REVAKALLRELLPPAAGFKCKVIFHDVAVLTDKLFPVVEAMQKYFSAGSGTYYSDSIFFL
SVAMHQIMPKEIPRIIQLDLDLKYKTNIRELFEEFDNFLPGAVIGIAREMQPVYRHTFWQ
FRHENPKTRVGDPPPEGLPGFNSGVMLLNLEAMRQSPLYSHLLEPSWVQQLADKYHFRGH
LGDQDFFTMIGMEHPELFHVLDCTWNRQLCTWWRDHGYSDVFQAYFRCEGHVKIYHGNCN
TPIPED

Primary citation

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:

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