Crystal structure of the human DEAH-helicase DHX15 in complex with the NKRF G-patch bound to ADP. Determined by X-ray diffraction at 1.85 Å resolution. Released 22 Apr 2020.
Explore 6SH6 in 3D Show helices and sheets RCSB PDB PDBe
6SH6 contains 46 α-helices and 30 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 | 116 | 1 | 1 |
| β-strand | 121 | 1 | 1 |
| α-helix | 122-124 | 3 | |
| α-helix | 125-134 | 10 | |
| α-helix | 138-142 | 5 | |
| α-helix | 143-150 | 8 | |
| β-strand | 155-159 | 5 | 2 |
| α-helix | 166-179 | 14 | |
| β-strand | 187-192 | 6 | 2 |
| α-helix | 195-208 | 14 | |
| β-strand | 213 | 1 | 2 |
| β-strand | 217-221 | 5 | 2 |
| β-strand | 224-226 | 3 | 2 |
| β-strand | 233-237 | 5 | 2 |
| α-helix | 238-245 | 8 | |
| β-strand | 254-259 | 6 | 2 |
| α-helix | 262-264 | 3 | |
| α-helix | 267-282 | 16 | |
| β-strand | 287-292 | 6 | 2 |
| α-helix | 296-298 | 3 | |
| α-helix | 299-303 | 5 | |
| β-strand | 309-311 | 3 | 2 |
| α-helix | 312-314 | 3 | |
| α-helix | 316-318 | 3 | |
| β-strand | 319-323 | 5 | 3 |
| α-helix | 331-345 | 15 | |
| β-strand | 351-355 | 5 | 3 |
| α-helix | 359-374 | 16 | |
| α-helix | 381-382 | 2 | |
| β-strand | 383-388 | 6 | 3 |
| α-helix | 394-397 | 4 | |
| α-helix | 398-401 | 4 | |
| α-helix | 403-406 | 4 | |
| β-strand | 415-420 | 6 | 3 |
| α-helix | 423-426 | 4 | |
| β-strand | 433-438 | 6 | 3 |
| β-strand | 441-448 | 8 | 4 |
| β-strand | 453-460 | 8 | 4 |
| α-helix | 461-462 | 2 | |
| α-helix | 463-471 | 9 | |
| α-helix | 472-474 | 3 | |
| β-strand | 479-483 | 5 | 3 |
| α-helix | 487-493 | 7 | |
| α-helix | 498-500 | 3 | |
| α-helix | 501-503 | 3 | |
| α-helix | 508-516 | 9 | |
| α-helix | 530-532 | 3 | |
| α-helix | 533-545 | 13 | |
| β-strand | 549 | 1 | 5 |
| α-helix | 554 | 1 | |
| β-strand | 555 | 1 | 5 |
| α-helix | 556 | 1 | |
| α-helix | 557-563 | 7 | |
| α-helix | 569-578 | 10 | |
| α-helix | 579-581 | 3 | |
| α-helix | 584-594 | 11 | |
| β-strand | 600 | 1 | 6 |
| α-helix | 607-615 | 9 | |
| β-strand | 619 | 1 | 7 |
| β-strand | 622 | 1 | 7 |
| α-helix | 623-636 | 14 | |
| α-helix | 641-646 | 6 | |
| β-strand | 649 | 1 | 6 |
| α-helix | 651-670 | 20 | |
| α-helix | 684-697 | 14 | |
| β-strand | 701-704 | 4 | 7 |
| β-strand | 710-712 | 3 | 7 |
| β-strand | 718-721 | 4 | 7 |
| β-strand | 733-741 | 9 | 7 |
| β-strand | 745-752 | 8 | 7 |
| α-helix | 755-761 | 7 | |
| α-helix | 771-772 | 2 | |
| α-helix | 775-788 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 554-561 | 8 | |
| α-helix | 582-586 | 5 | |
| α-helix | 589-590 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15 | A | protein | 689 | Homo sapiens | O43143 (AlphaFold model) |
| NF-kappa-B-repressing factor | B | protein | 67 | Homo sapiens | O15226 (AlphaFold model) |
>6SH6_1 Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15 (chains A) GPHMLEQCINPFTNLPHTPRYYDILKKRLQLPVWEYKDRFTDILVRHQSFVLVGETGSGK TTQIPQWCVEYMRSLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQEVGYSIRFEDC SSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDL KVIVMSATLDAGKFQIYFDNCPLLTIPGRTHPVEIFYTPEPERDYLEAAIRTVIQIHMCE EEEGDLLLFLTGQEEIDEACKRIKREVDDLGPEVGDIKIIPLYSTLPPQQQQRIFEPPPP KKQNGAIGRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYNPRIRVESLLVTAISKASA QQRAGRAGRTRPGKCFRLYTEKAYKTEMQDNTYPEILRSNLGSVVLQLKKLGIDDLVHFD FMDPPAPETLMRALELLNYLAALNDDGDLTELGSMMAEFPLDPQLAKMVIASCDYNCSNE VLSITAMLSVPQCFVRPTEAKKAADEAKMRFAHIDGDHLTLLNVYHAFKQNHESVQWCYD NFINYRSLMSADNVRQQLSRIMDRFNLPRRSTDFTSRDYYINIRKALVTGYFMQVAHLER TGHYLTVKDNQVVQLHPSTVLDHKPEWVLYNEFVLTTKNYIRTCTDIKPEWLVKIAPQYY DMSNFPQCEAKRQLDRIIAKLQSKEYSQY
>6SH6_2 NF-kappa-B-repressing factor (chains B) GPHMAEEAYKQQIKEDNIGNQLLRKMGWTGGGLGKSGEGIREPISVKEQHKREGLGLDVE RVNKIAK
Water and common crystallization additives (EDO) are not listed.
Structural basis for DEAH-helicase activation by G-patch proteins. Studer, M.K., Ivanovic, L., Weber, M.E. et al. Proc Natl Acad Sci U S A (2020) 117:7159-7170. DOI 10.1073/pnas.1913880117 · PubMed
Other PDB entries of the same protein (UniProt O43143 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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