Native structure of LSD2 /AOF1/KDM1b in spacegroup of C2221 at 2.13A. Determined by X-ray diffraction at 2.13 Å resolution. Released 16 Jan 2013.
Explore 4FWE in 3D Show helices and sheets RCSB PDB PDBe
4FWE contains 46 α-helices and 37 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 |
|---|---|---|---|
| β-strand | 65 | 1 | 1 |
| β-strand | 82-86 | 5 | 1 |
| β-strand | 89-92 | 4 | 1 |
| α-helix | 93-100 | 8 | |
| α-helix | 107-120 | 14 | |
| α-helix | 127-130 | 4 | |
| α-helix | 131-135 | 5 | |
| α-helix | 137-138 | 2 | |
| β-strand | 139-141 | 3 | 2 |
| β-strand | 150-152 | 3 | 2 |
| α-helix | 153-154 | 2 | |
| α-helix | 157-159 | 3 | |
| α-helix | 161-166 | 6 | |
| α-helix | 184-186 | 3 | |
| α-helix | 188-190 | 3 | |
| α-helix | 191-196 | 6 | |
| α-helix | 199-203 | 5 | |
| β-strand | 211 | 1 | 3 |
| α-helix | 217-219 | 3 | |
| α-helix | 225-228 | 4 | |
| β-strand | 230 | 1 | 3 |
| β-strand | 272 | 1 | 4 |
| α-helix | 273-274 | 2 | |
| β-strand | 284 | 1 | 4 |
| 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 | 378-380 | 3 | |
| β-strand | 384-388 | 5 | 5 |
| α-helix | 392-404 | 13 | |
| β-strand | 407-411 | 5 | 5 |
| β-strand | 423-424 | 2 | 6 |
| β-strand | 432-433 | 2 | 6 |
| β-strand | 438-440 | 3 | 7 |
| α-helix | 446-454 | 9 | |
| β-strand | 459-460 | 2 | 7 |
| β-strand | 467-468 | 2 | 8 |
| α-helix | 469 | 1 | |
| α-helix | 473 | 1 | |
| β-strand | 474 | 1 | 8 |
| α-helix | 475-476 | 2 | |
| α-helix | 477-498 | 22 | |
| α-helix | 503-505 | 3 | |
| β-strand | 508 | 1 | 9 |
| α-helix | 509-522 | 14 | |
| α-helix | 530-547 | 18 | |
| β-strand | 554 | 1 | 10 |
| β-strand | 555 | 1 | 9 |
| α-helix | 561-564 | 4 | |
| α-helix | 566-569 | 4 | |
| β-strand | 572-574 | 3 | 7 |
| α-helix | 579-587 | 9 | |
| β-strand | 592-593 | 2 | 5 |
| β-strand | 598-602 | 5 | 11 |
| β-strand | 608-612 | 5 | 11 |
| β-strand | 617-620 | 4 | 11 |
| β-strand | 622-625 | 4 | 5 |
| α-helix | 629-633 | 5 | |
| β-strand | 638-640 | 3 | 11 |
| α-helix | 642-644 | 3 | |
| α-helix | 645-653 | 9 | |
| β-strand | 654-657 | 4 | 12 |
| β-strand | 660-665 | 6 | 8 |
| α-helix | 672-675 | 4 | |
| β-strand | 680-683 | 4 | 8 |
| α-helix | 688-690 | 3 | |
| β-strand | 693-699 | 7 | 8 |
| β-strand | 708-713 | 6 | 8 |
| α-helix | 716-721 | 6 | |
| α-helix | 726-740 | 15 | |
| α-helix | 747-749 | 3 | |
| β-strand | 751-754 | 4 | 8 |
| α-helix | 757-759 | 3 | |
| β-strand | 767-770 | 4 | 12 |
| β-strand | 771 | 1 | 10 |
| α-helix | 777-783 | 7 | |
| β-strand | 786 | 1 | 5 |
| β-strand | 790-792 | 3 | 5 |
| α-helix | 795-797 | 3 | |
| α-helix | 805-821 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lysine-specific histone demethylase 1B | A | protein | 796 | Homo sapiens | Q8NB78 (AlphaFold model) |
>4FWE_1 Lysine-specific histone demethylase 1B (chains A) GHMAKKKATETTDEDEDGGSEKKYRKCEKAGCTATCPVCFASASERCAKNGYTSRWYHLS CGEHFCNECFDHYYRSHKDGYDKYTTWKKIWTSNGKTEPSPKAFMADQQLPYWVQCTKPE CRKWRQLTKEIQLTPQIAKTYRCGMKPNTAIKPETSDHCSLPEDLRVLEVSNHWWYSMLI LPPLLKDSVAAPLLSAYYPDCVGMSPSCTSTNRAAATGNASPGKLEHSKAALSVHVPGMN RYFQPFYQPNECGKALCVRPDVMELDELYEFPEYSRDPTMYLALRNLILALWYTNCKEAL TPQKCIPHIIVRGLVRIRCVQEVERILYFMTRKGLINTGVLSVGADQYLLPKDYHNKSVI IIGAGPAGLAAARQLHNFGIKVTVLEAKDRIGGRVWDDKSFKGVTVGRGAQIVNGCINNP VALMCEQLGISMHKFGERCDLIQEGGRITDPTIDKRMDFHFNALLDVVSEWRKDKTQLQD VPLGEKIEEIYKAFIKESGIQFSELEGQVLQFHLSNLEYACGSNLHQVSARSWDHNEFFA QFAGDHTLLTPGYSVIIEKLAEGLDIQLKSPVQCIDYSGDEVQVTTTDGTGYSAQKVLVT VPLALLQKGAIQFNPPLSEKKMKAINSLGAGIIEKIALQFPYRFWDSKVQGADFFGHVPP SASKRGLFAVFYDMDPQKKHSVLMSVIAGEAVASVRTLDDKQVLQQCMATLRELFKEQEV PDPTKYFVTRWSTDPWIQMAYSFVKTGGSGEAYDIIAEDIQGTVFFAGEATNRHFPQTVT GAYLSGVREASKIAAF
| ID | Name | Formula | Copies |
|---|---|---|---|
| FLC | Citrate anion | C6 H5 O7 | 1 |
| FAD | Flavin-adenine dinucleotide | C27 H33 N9 O15 P2 | 1 |
| ZN | Zinc ion | Zn | 3 |
Structure-function analysis reveals a novel mechanism for regulation of histone demethylase LSD2/AOF1/KDM1b. Zhang, Q., Qi, S., Xu, M. et al. Cell Res (2013) 23:225-241. DOI 10.1038/cr.2012.177 · 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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