Aspartyl/Asparaginyl beta-hydroxylase (AspH) in complex with Mn, 2OG, thiocyanate and Factor X peptide fragment (39mer-4Ser). Determined by X-ray diffraction at 1.6 Å resolution. Released 24 Dec 2025.
Explore 9FVV in 3D Show helices and sheets RCSB PDB PDBe
9FVV contains 22 α-helices and 18 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 | 336-340 | 5 | |
| α-helix | 342-353 | 12 | |
| α-helix | 357-370 | 14 | |
| α-helix | 375-392 | 18 | |
| α-helix | 395-410 | 16 | |
| α-helix | 416-432 | 17 | |
| α-helix | 436-449 | 14 | |
| α-helix | 454-466 | 13 | |
| α-helix | 470-483 | 14 | |
| α-helix | 488-500 | 13 | |
| α-helix | 504-517 | 14 | |
| α-helix | 525-538 | 14 | |
| α-helix | 543-552 | 10 | |
| β-strand | 561 | 1 | 1 |
| β-strand | 565 | 1 | 2 |
| β-strand | 575-576 | 2 | 3 |
| α-helix | 578-581 | 4 | |
| α-helix | 584-592 | 9 | |
| α-helix | 594-607 | 14 | |
| α-helix | 609-611 | 3 | |
| β-strand | 613-614 | 2 | 3 |
| β-strand | 620-622 | 3 | 4 |
| β-strand | 625-632 | 8 | 3 |
| β-strand | 635-636 | 2 | 3 |
| α-helix | 638-643 | 6 | |
| α-helix | 645-651 | 7 | |
| α-helix | 655-658 | 4 | |
| β-strand | 664-670 | 7 | 3 |
| β-strand | 674-679 | 6 | 4 |
| β-strand | 683 | 1 | 2 |
| β-strand | 686-694 | 9 | 3 |
| β-strand | 700-704 | 5 | 4 |
| β-strand | 707-709 | 3 | 4 |
| β-strand | 713 | 1 | 3 |
| β-strand | 716-719 | 4 | 3 |
| β-strand | 723 | 1 | 1 |
| β-strand | 725-729 | 5 | 4 |
| β-strand | 735-743 | 9 | 3 |
| α-helix | 749-754 | 6 | |
| α-helix | 756-757 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Aspartyl/asparaginyl beta-hydroxylase | A | protein | 429 | Homo sapiens | Q12797 (AlphaFold model) |
| Factor X light chain | B | protein | 39 | Homo sapiens | P00742 (AlphaFold model) |
>9FVV_1 Aspartyl/asparaginyl beta-hydroxylase (chains A) KPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLA EKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGHMRGSLLTLQRLVQL FPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIP YLKEGIESGDPGTDDGRFYFHLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNG LKAQPWWTPKETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFT LWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPHTGPTNCRLRM HLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHPELTP QQRRSLPAI
>9FVV_2 Factor X light chain (chains B) DGDQSETSPSQNQGKCKNGLGEYTCTSLEGFEGKNSELF
Water and common crystallization additives (ACT, PEG) are not listed.
Structural basis of the promiscuity of the unusual Fe(II) and 2-oxoglutarate dependent human aspartate/asparagine-beta-hydroxylase. de Munnik, M., Brasnett, A., Zhou, T. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-69425-w · PubMed
Other PDB entries of the same protein (UniProt Q12797 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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