Crystal structure of LSD2-NPAC. Determined by X-ray diffraction at 2.0 Å resolution. Released 16 Jan 2013.
Explore 4GUT in 3D Show helices and sheets RCSB PDB PDBe
4GUT contains 49 α-helices and 40 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 | 50 | 1 | 1 |
| β-strand | 53 | 1 | 2 |
| β-strand | 65 | 1 | 2 |
| β-strand | 79 | 1 | 1 |
| β-strand | 82-86 | 5 | 2 |
| β-strand | 89-92 | 4 | 2 |
| α-helix | 93-100 | 8 | |
| α-helix | 107-119 | 13 | |
| α-helix | 127-130 | 4 | |
| α-helix | 131-135 | 5 | |
| α-helix | 137-138 | 2 | |
| β-strand | 139-141 | 3 | 3 |
| β-strand | 150-152 | 3 | 3 |
| α-helix | 153-154 | 2 | |
| α-helix | 161-166 | 6 | |
| α-helix | 184-186 | 3 | |
| α-helix | 188-190 | 3 | |
| α-helix | 191-195 | 5 | |
| β-strand | 211 | 1 | 4 |
| α-helix | 217-219 | 3 | |
| α-helix | 225-227 | 3 | |
| β-strand | 230 | 1 | 4 |
| β-strand | 272 | 1 | 5 |
| α-helix | 273-274 | 2 | |
| α-helix | 277-279 | 3 | |
| β-strand | 284 | 1 | 5 |
| α-helix | 291-296 | 6 | |
| α-helix | 298-300 | 3 | |
| α-helix | 305-320 | 16 | |
| α-helix | 328-331 | 4 | |
| α-helix | 332-334 | 3 | |
| α-helix | 341-359 | 19 | |
| α-helix | 371-373 | 3 | |
| α-helix | 378-380 | 3 | |
| β-strand | 384-388 | 5 | 6 |
| α-helix | 392-404 | 13 | |
| β-strand | 407-411 | 5 | 6 |
| β-strand | 423-424 | 2 | 7 |
| β-strand | 432-433 | 2 | 7 |
| β-strand | 438-440 | 3 | 8 |
| α-helix | 446-454 | 9 | |
| β-strand | 459-460 | 2 | 8 |
| α-helix | 461-462 | 2 | |
| β-strand | 467-468 | 2 | 9 |
| α-helix | 469 | 1 | |
| α-helix | 473 | 1 | |
| β-strand | 474 | 1 | 9 |
| α-helix | 475-476 | 2 | |
| α-helix | 477-497 | 21 | |
| α-helix | 498-500 | 3 | |
| α-helix | 503-505 | 3 | |
| β-strand | 508 | 1 | 10 |
| α-helix | 509-523 | 15 | |
| α-helix | 526-529 | 4 | |
| α-helix | 530-547 | 18 | |
| β-strand | 554 | 1 | 11 |
| β-strand | 555 | 1 | 10 |
| α-helix | 561-564 | 4 | |
| β-strand | 572-574 | 3 | 8 |
| α-helix | 580-587 | 8 | |
| β-strand | 592-593 | 2 | 6 |
| β-strand | 598-602 | 5 | 12 |
| β-strand | 608-612 | 5 | 12 |
| β-strand | 617-620 | 4 | 12 |
| β-strand | 622-625 | 4 | 6 |
| α-helix | 629-633 | 5 | |
| β-strand | 638-640 | 3 | 12 |
| α-helix | 642-644 | 3 | |
| α-helix | 645-653 | 9 | |
| β-strand | 654-657 | 4 | 13 |
| β-strand | 660-665 | 6 | 9 |
| α-helix | 672-675 | 4 | |
| β-strand | 680-683 | 4 | 9 |
| α-helix | 688-690 | 3 | |
| β-strand | 693-699 | 7 | 9 |
| β-strand | 708-713 | 6 | 9 |
| α-helix | 716-722 | 7 | |
| α-helix | 726-740 | 15 | |
| α-helix | 747-749 | 3 | |
| β-strand | 751-754 | 4 | 9 |
| α-helix | 757-759 | 3 | |
| β-strand | 767-770 | 4 | 13 |
| β-strand | 771 | 1 | 11 |
| α-helix | 777-783 | 7 | |
| β-strand | 786 | 1 | 6 |
| β-strand | 790-792 | 3 | 6 |
| α-helix | 795-797 | 3 | |
| α-helix | 805-820 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 220-222 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lysine-specific histone demethylase 1B | A | protein | 776 | Homo sapiens | Q8NB78 (AlphaFold model) |
| Putative oxidoreductase GLYR1 | B | protein | 124 | Homo sapiens | Q49A26 (AlphaFold model) |
>4GUT_1 Lysine-specific histone demethylase 1B (chains A) PLGSRKCEKAGCTATCPVCFASASERCAKNGYTSRWYHLSCGEHFCNECFDHYYRSHKDG YDKYTTWKKIWTSNGKTEPSPKAFMADQQLPYWVQCTKPECRKWRQLTKEIQLTPQIAKT YRCGMKPNTAIKPETSDHCSLPEDLRVLEVSNHWWYSMLILPPLLKDSVAAPLLSAYYPD CVGMSPSCTSTNRAAATGNASPGKLEHSKAALSVHVPGMNRYFQPFYQPNECGKALCVRP DVMELDELYEFPEYSRDPTMYLALRNLILALWYTNCKEALTPQKCIPHIIVRGLVRIRCV QEVERILYFMTRKGLINTGVLSVGADQYLLPKDYHNKSVIIIGAGPAGLAAARQLHNFGI KVTVLEAKDRIGGRVWDDKSFKGVTVGRGAQIVNGCINNPVALMCEQLGISMHKFGERCD LIQEGGRITDPTIDKRMDFHFNALLDVVSEWRKDKTQLQDVPLGEKIEEIYKAFIKESGI QFSELEGQVLQFHLSNLEYACGSNLHQVSARSWDHNEFFAQFAGDHTLLTPGYSVIIEKL AEGLDIQLKSPVQCIDYSGDEVQVTTTDGTGYSAQKVLVTVPLALLQKGAIQFNPPLSEK KMKAINSLGAGIIEKIALQFPYRFWDSKVQGADFFGHVPPSASKRGLFAVFYDMDPQKKH SVLMSVIAGEAVASVRTLDDKQVLQQCMATLRELFKEQEVPDPTKYFVTRWSTDPWIQMA YSFVKTGGSGEAYDIIAEDIQGTVFFAGEATNRHFPQTVTGAYLSGVREASKIAAF
>4GUT_2 Putative oxidoreductase GLYR1 (chains B) PLGSPEFSERGSKSPLKRAQEQSPRKRGRPPKDEKDLTIPESSTVKGMMAGPMAAFKWQP TASEPVKDADPHFHHFLLSQTEKPAVCYQAITKKLKICEEETGSTSIQAADSTAVNGSIT PTDK
Water and common crystallization additives (GOL, PGE) are not listed.
LSD2/KDM1B and its cofactor NPAC/GLYR1 endow a structural and molecular model for regulation of H3K4 demethylation. Fang, R., Chen, F., Dong, Z. et al. Mol Cell (2013) 49:558-570. DOI 10.1016/j.molcel.2012.11.019 · PubMed
Other PDB entries of the same protein (UniProt Q8NB78 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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