Structural Basis of Human NOX5 Activation. Determined by electron microscopy at 3.3 Å resolution. Released 1 May 2024.
Explore 8U86 in 3D Show helices and sheets RCSB PDB PDBe
8U86 contains 36 α-helices and 36 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 |
|---|---|---|---|
| α-helix | 184-188 | 5 | |
| α-helix | 192-212 | 21 | |
| α-helix | 221-241 | 21 | |
| α-helix | 246-250 | 5 | |
| α-helix | 254-258 | 5 | |
| α-helix | 264-293 | 30 | |
| α-helix | 321-337 | 17 | |
| α-helix | 341-345 | 5 | |
| α-helix | 349-356 | 8 | |
| α-helix | 359-367 | 9 | |
| α-helix | 373-390 | 18 | |
| β-strand | 397-398 | 2 | 1 |
| β-strand | 401 | 1 | 2 |
| β-strand | 402-408 | 7 | 3 |
| β-strand | 412-418 | 7 | 3 |
| α-helix | 419-420 | 2 | |
| β-strand | 430-433 | 4 | 4 |
| β-strand | 444-447 | 4 | 4 |
| β-strand | 448 | 1 | 3 |
| β-strand | 457-463 | 7 | 3 |
| α-helix | 469-477 | 9 | |
| β-strand | 518 | 1 | 2 |
| β-strand | 521-522 | 2 | 1 |
| β-strand | 525 | 1 | 4 |
| α-helix | 530-533 | 4 | |
| β-strand | 538-543 | 6 | 5 |
| α-helix | 548-562 | 15 | |
| β-strand | 565-567 | 3 | 6 |
| β-strand | 574-576 | 3 | 6 |
| β-strand | 588-593 | 6 | 5 |
| α-helix | 601-615 | 15 | |
| β-strand | 624-629 | 6 | 5 |
| β-strand | 668 | 1 | 5 |
| α-helix | 674-683 | 10 | |
| β-strand | 690-694 | 5 | 5 |
| α-helix | 697-708 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| NADPH oxidase 5 | A, C | protein | 719 | Homo sapiens | Q96PH1 (AlphaFold model) |
>8U86_1 NADPH oxidase 5 (chains A, C) MSAEEDARWLRWVTQQFKTIAGEDGEISLQEFKAALHVKESFFAERFFALFDSDRSGTIT LQELQEALTLLIHGSPMDKLKFLFQVYDIDGSGSIDPDELRTVLQSCLRESAISLPDEKL DQLTLALFESADADGNGAITFEELRDELQRFPGVMENLTISAAHWLTAPAPRPRPRRPRQ LTRAYWHNHRSQLFCLATYAGLHVLLFGLAASAHRDLGASVMVAKGCGQCLNFDCSFIAV LMLRRCLTWLRATWLAQVLPLDQNIQFHQLMGYVVVGLSLVHTVAHTVNFVLQAQAEASP FQFWELLLTTRPGIGWVHGSASPTGVALLLLLLLMFICSSSCIRRSGHFEVFYWTHLSYL LVWLLLIFHGPNFWKWLLVPGILFFLEKAIGLAVSRMAAVCIMEVNLLPSKVTHLLIKRP PFFHYRPGDYLYLNIPTIARYEWHPFTISSAPEQKDTIWLHIRSQGQWTNRLYESFKASD PLGRGSKRLSRSVTMRKSQRSSKGSEILLEKHKFCNIKCYIDGPYGTPTRRIFASEHAVL IGAGIGITPFASILQSIMYRHQKRKHTCPSCQHSWIEGVQDNMKLHKVDFIWINRDQRSF EWFVSLLTKLEMDQAEEAQYGRFLELHMYMTSALGKNDMKAIGLQMALDLLANKEKKDSI TGLQTRTQPGRPDWSKVFQKVAAEKKGKVQVFFCGSPALAKVLKGHCEKFGFRFFQENF
| ID | Name | Formula | Copies |
|---|---|---|---|
| D10 | Decane | C10 H22 | 2 |
| ZN | Zinc ion | Zn | 1 |
| D12 | Dodecane | C12 H26 | 2 |
| FAD | Flavin-adenine dinucleotide | C27 H33 N9 O15 P2 | 2 |
| NDP | NADPH dihydro-nicotinamide-adenine-dinucleotide phosphate | C21 H30 N7 O17 P3 | 2 |
| HEB | Heme b/c | C34 H34 Fe N4 O4 | 4 |
Structural basis of human NOX5 activation. Cui, C., Jiang, M., Jain, N. et al. Nat Commun (2024) 15:3994-3994. DOI 10.1038/s41467-024-48467-y · PubMed
Other PDB entries of the same protein (UniProt Q96PH1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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