Crystal structure of ribosomal oxygenase NO66 dimer mutant. Determined by X-ray diffraction at 3.3 Å resolution. Released 7 Oct 2015.
Explore 4Y4R in 3D Show helices and sheets RCSB PDB PDBe
4Y4R contains 45 α-helices and 46 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 | 184-192 | 9 | |
| α-helix | 198-210 | 13 | |
| α-helix | 215-217 | 3 | |
| α-helix | 218-222 | 5 | |
| β-strand | 228-230 | 3 | 1 |
| α-helix | 244-253 | 10 | |
| β-strand | 258 | 1 | 1 |
| β-strand | 262-268 | 7 | 1 |
| β-strand | 271-274 | 4 | 1 |
| α-helix | 283-291 | 9 | |
| α-helix | 294 | 1 | |
| β-strand | 295-298 | 4 | 1 |
| α-helix | 301-304 | 4 | |
| α-helix | 306-319 | 14 | |
| β-strand | 324-330 | 7 | 1 |
| β-strand | 340-341 | 2 | 2 |
| β-strand | 345-353 | 9 | 1 |
| β-strand | 355-360 | 6 | 2 |
| α-helix | 365-367 | 3 | |
| α-helix | 373-377 | 5 | |
| α-helix | 379-381 | 3 | |
| β-strand | 387-391 | 5 | 2 |
| β-strand | 396-399 | 4 | 1 |
| β-strand | 404-408 | 5 | 2 |
| β-strand | 415-422 | 8 | 1 |
| β-strand | 427 | 1 | 3 |
| α-helix | 428-446 | 19 | |
| α-helix | 448-450 | 3 | |
| β-strand | 453 | 1 | 4 |
| α-helix | 458-460 | 3 | |
| α-helix | 465-467 | 3 | |
| α-helix | 474-489 | 16 | |
| α-helix | 494-508 | 15 | |
| α-helix | 510-512 | 3 | |
| α-helix | 516-521 | 6 | |
| β-strand | 522 | 1 | 5 |
| β-strand | 535-538 | 4 | 5 |
| β-strand | 544-548 | 5 | 6 |
| β-strand | 553-557 | 5 | 6 |
| α-helix | 569-571 | 3 | |
| β-strand | 572-574 | 3 | 6 |
| α-helix | 580-588 | 9 | |
| β-strand | 594-595 | 2 | 5 |
| α-helix | 596-598 | 3 | |
| α-helix | 604-616 | 13 | |
| β-strand | 620-622 | 3 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 184-193 | 10 | |
| α-helix | 198-210 | 13 | |
| α-helix | 215-221 | 7 | |
| β-strand | 228-230 | 3 | 7 |
| α-helix | 244-253 | 10 | |
| β-strand | 257 | 1 | 8 |
| β-strand | 258 | 1 | 9 |
| β-strand | 262 | 1 | 9 |
| β-strand | 263-268 | 6 | 7 |
| β-strand | 271-274 | 4 | 7 |
| β-strand | 280 | 1 | 8 |
| α-helix | 283-291 | 9 | |
| β-strand | 295-299 | 5 | 7 |
| α-helix | 306-319 | 14 | |
| β-strand | 324-330 | 7 | 7 |
| β-strand | 335 | 1 | 7 |
| β-strand | 340 | 1 | 10 |
| β-strand | 345-353 | 9 | 7 |
| β-strand | 355-359 | 5 | 10 |
| α-helix | 365-367 | 3 | |
| α-helix | 374-377 | 4 | |
| β-strand | 387-391 | 5 | 10 |
| β-strand | 396-399 | 4 | 7 |
| β-strand | 405-408 | 4 | 10 |
| β-strand | 415-422 | 8 | 7 |
| β-strand | 427 | 1 | 4 |
| α-helix | 428-446 | 19 | |
| α-helix | 449-451 | 3 | |
| β-strand | 453 | 1 | 3 |
| α-helix | 454-455 | 2 | |
| α-helix | 458-460 | 3 | |
| α-helix | 464-466 | 3 | |
| α-helix | 474-491 | 18 | |
| α-helix | 494-508 | 15 | |
| α-helix | 510-515 | 6 | |
| α-helix | 516-521 | 6 | |
| β-strand | 538 | 1 | 11 |
| β-strand | 544-547 | 4 | 12 |
| β-strand | 554-557 | 4 | 12 |
| α-helix | 569-570 | 2 | |
| β-strand | 572-574 | 3 | 12 |
| α-helix | 577-588 | 12 | |
| α-helix | 596-598 | 3 | |
| α-helix | 604-616 | 13 | |
| β-strand | 620 | 1 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66 | A, B | protein | 454 | Homo sapiens | Q9H6W3 (AlphaFold model) |
>4Y4R_1 Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66 (chains A, B) GGEPAWDSPLRRVLAELNRIPSSRRRAARLFEWLIAPMPPDHFYRRLWEREAVLVRRQDH TYYQGLFSTADLDSMLRNEEVQFGQHLDAARYINGRRETLNPPGRALPAAAWSLYQAGCS LRLLCPQAFSTTVWQFLAVLQEQFGSMAGSNVYLTPPNSQGFAPHYDDIEAFVLQLEGRK LWRVYRPRVPTEELALTSSPNFSQDDLGEPVLQTVLEPGDLLYFPRGFIHQAECQDGVHS LHLTLSTYQRNTWGDFLEAILPLAVQAAMEENVEFRRGLPRDFMDYMGAQHSDSKDPRRT AFMEKVRVLVARLGHFAPVDAVADQRAKDFIHDSLPPVLTDRERALSVYGGGGQLTTETE VHMLQDGIARLVGEGGHLFLYYTVENSRVYHLEEPKCLEIYPQQADAMELLLGSYPEFVR VGDLPCDSVEDQLSLATTLYDKGLLLTKMPLALN
| ID | Name | Formula | Copies |
|---|---|---|---|
| NI | Nickel (II) ion | Ni | 2 |
Water and common crystallization additives (ACT) are not listed.
Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8. Wang, C., Zhang, Q., Hang, T. et al. Acta Crystallogr D Biol Crystallogr (2015) 71:1955-1964. DOI 10.1107/S1399004715012948 · PubMed
Other PDB entries of the same protein (UniProt Q9H6W3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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