Human Xylosyltransferase 1 apo structure. Determined by X-ray diffraction at 1.87 Å resolution. Released 2 May 2018.
Explore 6FOA in 3D Show helices and sheets RCSB PDB PDBe
6FOA contains 36 α-helices and 35 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 | 262-270 | 9 | |
| α-helix | 274-288 | 15 | |
| β-strand | 296 | 1 | 1 |
| α-helix | 315-318 | 4 | |
| β-strand | 328-334 | 7 | 2 |
| α-helix | 339-349 | 11 | |
| β-strand | 355-360 | 6 | 2 |
| α-helix | 365-377 | 13 | |
| β-strand | 381-383 | 3 | 2 |
| α-helix | 396-410 | 15 | |
| β-strand | 418-422 | 5 | 2 |
| β-strand | 426-428 | 3 | 3 |
| α-helix | 432-441 | 10 | |
| β-strand | 446-448 | 3 | 2 |
| β-strand | 450 | 1 | 4 |
| α-helix | 455-462 | 8 | |
| β-strand | 466-471 | 6 | 5 |
| β-strand | 474-480 | 7 | 5 |
| α-helix | 482-484 | 3 | |
| β-strand | 485 | 1 | 1 |
| β-strand | 492 | 1 | 4 |
| β-strand | 497-499 | 3 | 2 |
| α-helix | 500-508 | 9 | |
| α-helix | 512-520 | 9 | |
| α-helix | 521-523 | 3 | |
| α-helix | 527-529 | 3 | |
| α-helix | 531-538 | 8 | |
| α-helix | 542-544 | 3 | |
| β-strand | 545-547 | 3 | 2 |
| β-strand | 551-553 | 3 | 3 |
| α-helix | 557-560 | 4 | |
| β-strand | 569 | 1 | 5 |
| α-helix | 576-579 | 4 | |
| α-helix | 581-588 | 8 | |
| β-strand | 596-598 | 3 | 3 |
| α-helix | 607-617 | 11 | |
| α-helix | 619-621 | 3 | |
| β-strand | 629-636 | 8 | 6 |
| α-helix | 637-639 | 3 | |
| α-helix | 641-643 | 3 | |
| α-helix | 646-665 | 20 | |
| β-strand | 677-691 | 15 | 6 |
| β-strand | 694-706 | 13 | 6 |
| β-strand | 711-721 | 11 | 6 |
| α-helix | 722-723 | 2 | |
| β-strand | 726-727 | 2 | 7 |
| β-strand | 737-743 | 7 | 8 |
| β-strand | 746-747 | 2 | 9 |
| β-strand | 752-753 | 2 | 9 |
| β-strand | 767-772 | 6 | 8 |
| β-strand | 778-785 | 8 | 7 |
| β-strand | 791-799 | 9 | 7 |
| β-strand | 805-808 | 4 | 8 |
| α-helix | 816-817 | 2 | |
| β-strand | 819-827 | 9 | 7 |
| β-strand | 830-839 | 10 | 7 |
| α-helix | 840-842 | 3 | |
| β-strand | 844-845 | 2 | 10 |
| β-strand | 848-849 | 2 | 10 |
| α-helix | 850-851 | 2 | |
| α-helix | 852-859 | 8 | |
| α-helix | 873-875 | 3 | |
| α-helix | 882-884 | 3 | |
| α-helix | 885-895 | 11 | |
| α-helix | 899-913 | 15 | |
| β-strand | 914-921 | 8 | 6 |
| α-helix | 930 | 1 | |
| β-strand | 931-932 | 2 | 6 |
| α-helix | 933-935 | 3 | |
| α-helix | 945-947 | 3 | |
| α-helix | 951-953 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Xylosyltransferase 1 | A | protein | 751 | Homo sapiens | Q86Y38 (AlphaFold model) |
>6FOA_1 Xylosyltransferase 1 (chains A) APLVHHHHHHALDENLYFQGALADVSRPPHARKTGGSSPETKYDQPPKCDISGKEAISAL SRAKSKHCRQEIGETYCRHKLGLLMPEKVTRFCPLEGKANKNVQWDEDSVEYMPANPVRI AFVLVVHGRASRQLQRMFKAIYHKDHFYYIHVDKRSNYLHRQVLQVSRQYSNVRVTPWRM ATIWGGASLLSTYLQSMRDLLEMTDWPWDFFINLSAADYPIRTNDQLVAFLSRYRDMNFL KSHGRDNARFIRKQGLDRLFLECDAHMWRLGDRRIPEGIAVDGGSDWFLLNRRFVEYVTF STDDLVTKMKQFYSYTLLPAESFFHTVLENSPHCDTMVDNNLRITNWNRKLGCKCQYKHI VDWCGCSPNDFKPQDFHRFQQTARPTFFARKFEAVVNQEIIGQLDYYLYGNYPAGTPGLR SYWENVYDEPDGIHSLSDVTLTLYHSFARLGLRRAETSLHTDGENSCRYYPMGHPASVHL YFLADRFQGFLIKHHATNLAVSKLETLETWVMPKKVFKIASPPSDFGRLQFSEVGTDWDA KERLFRNFGGLLGPMDEPVGMQKWGKGPNVTVTVIWVDPVNVIAATYDILIESTAEFTHY KPPLNLPLRPGVWTVKILHHWVPVAETKFLVAPLTFSNRQPIKPEEALKLHNGPLRNAYM EQSFQSLNPVLSLPINPAQVEQARRNAASTGTALEGWLDSLVGGMWTAMDICATGPTACP VMQTCSQTAWSSFSPDPKSELGAVKPDGRLR
Water and common crystallization additives (NA) are not listed.
Structural Basis for the Initiation of Glycosaminoglycan Biosynthesis by Human Xylosyltransferase 1. Briggs, D.C., Hohenester, E. Structure (2018) 26:801-809.e3. DOI 10.1016/j.str.2018.03.014 · PubMed
Other PDB entries of the same protein (UniProt Q86Y38 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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