4FWJ: Lysine-specific histone demethylase 1B

Native structure of LSD2/AOF1/KDM1b in spacegroup of I222 at 2.9A. Determined by X-ray diffraction at 2.9 Å resolution. Released 16 Jan 2013.

Method
X-ray diffraction
Resolution
2.9 Å
Organism
Homo sapiens
Chains
2
Atoms
12,080
Mol. weight
180.78 kDa
Ligands
ZN, FAD, PO4
Released
16 Jan 2013

Explore 4FWJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4FWJ contains 94 α-helices and 78 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.

Chain A: 49 helices, 41 β-strands

ElementResiduesLengthSheet
β-strand5011
β-strand6512
β-strand7911
β-strand83-8422
β-strand90-9122
α-helix93-953
α-helix104-1063
α-helix107-12014
α-helix124-1252
α-helix127-1304
α-helix131-1355
α-helix137-1382
β-strand139-14133
β-strand150-15233
α-helix153-1542
α-helix157-1593
α-helix161-1666
α-helix184-1863
α-helix188-1892
α-helix192-1954
α-helix199-2035
β-strand21114
β-strand21215
α-helix217-2204
α-helix225-2284
β-strand23014
β-strand27216
α-helix273-2742
β-strand28416
α-helix291-2966
α-helix298-3003
α-helix305-32016
α-helix328-3314
α-helix332-3343
β-strand33615
α-helix342-35817
β-strand384-38857
α-helix392-40413
β-strand407-41157
β-strand423-42428
β-strand432-43328
β-strand438-44039
α-helix446-4549
β-strand459-46029
α-helix461-4622
β-strand467-468210
α-helix4691
α-helix4731
β-strand474110
α-helix475-4762
α-helix477-49721
α-helix498-5003
α-helix503-5053
β-strand508111
α-helix509-52416
α-helix530-54718
α-helix551-5533
β-strand554112
β-strand555111
α-helix561-5644
β-strand572-57439
α-helix579-5879
β-strand592-59327
β-strand598-602513
β-strand608-612513
β-strand617-620413
β-strand622-62547
α-helix629-6335
β-strand638-640313
α-helix642-6443
α-helix645-6539
β-strand654-657414
β-strand659-665710
α-helix672-6754
β-strand680-683410
α-helix688-6903
β-strand693-699710
β-strand708-714710
α-helix716-7205
α-helix726-74015
α-helix747-7493
β-strand751-754410
α-helix757-7593
β-strand767-770414
β-strand771112
α-helix777-7837
β-strand78617
β-strand790-79237
α-helix795-7973
α-helix805-82117
Chain B: 45 helices, 37 β-strands
ElementResiduesLengthSheet
α-helix63-642
β-strand65115
β-strand82-86515
β-strand89-92415
α-helix107-12014
α-helix124-1252
α-helix127-1348
β-strand139-141316
β-strand150-152316
α-helix153-1542
α-helix161-1666
α-helix188-1903
α-helix191-1977
α-helix202-2043
β-strand211117
α-helix217-2204
α-helix225-2284
β-strand230117
β-strand272118
α-helix278-2792
β-strand284118
α-helix291-2966
α-helix298-3003
α-helix305-32016
α-helix328-3314
α-helix332-3343
α-helix341-35919
α-helix367-3704
α-helix380-3823
β-strand384-388519
α-helix392-40413
β-strand407-411519
β-strand423-424220
β-strand432-433220
β-strand438-440321
α-helix446-4549
β-strand459-460221
α-helix461-4622
β-strand467-469322
α-helix4731
β-strand474122
α-helix475-4762
α-helix477-49721
α-helix498-5003
α-helix503-5053
β-strand508123
α-helix509-52416
α-helix530-54718
β-strand554124
β-strand555123
α-helix561-5644
α-helix566-5694
β-strand572-574321
α-helix579-5879
β-strand591-593319
β-strand598-602525
β-strand608-612525
β-strand617-620425
β-strand622-625419
α-helix629-6335
β-strand638-640325
α-helix642-6443
α-helix645-6539
β-strand654-657426
β-strand660-665622
α-helix672-6754
β-strand680-684522
α-helix688-6903
β-strand693-699722
β-strand708-713622
α-helix718-7214
α-helix726-74015
α-helix747-7493
β-strand752-754322
α-helix757-7593
β-strand767-770426
β-strand771124
α-helix778-7836
β-strand786119
β-strand790-792319
α-helix795-7973
α-helix805-82117

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Lysine-specific histone demethylase 1BA, Bprotein796Homo sapiensQ8NB78 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4FWJ_1 Lysine-specific histone demethylase 1B (chains A, B)
GHMAKKKATETTDEDEDGGSEKKYRKCEKAGCTATCPVCFASASERCAKNGYTSRWYHLS
CGEHFCNECFDHYYRSHKDGYDKYTTWKKIWTSNGKTEPSPKAFMADQQLPYWVQCTKPE
CRKWRQLTKEIQLTPQIAKTYRCGMKPNTAIKPETSDHCSLPEDLRVLEVSNHWWYSMLI
LPPLLKDSVAAPLLSAYYPDCVGMSPSCTSTNRAAATGNASPGKLEHSKAALSVHVPGMN
RYFQPFYQPNECGKALCVRPDVMELDELYEFPEYSRDPTMYLALRNLILALWYTNCKEAL
TPQKCIPHIIVRGLVRIRCVQEVERILYFMTRKGLINTGVLSVGADQYLLPKDYHNKSVI
IIGAGPAGLAAARQLHNFGIKVTVLEAKDRIGGRVWDDKSFKGVTVGRGAQIVNGCINNP
VALMCEQLGISMHKFGERCDLIQEGGRITDPTIDKRMDFHFNALLDVVSEWRKDKTQLQD
VPLGEKIEEIYKAFIKESGIQFSELEGQVLQFHLSNLEYACGSNLHQVSARSWDHNEFFA
QFAGDHTLLTPGYSVIIEKLAEGLDIQLKSPVQCIDYSGDEVQVTTTDGTGYSAQKVLVT
VPLALLQKGAIQFNPPLSEKKMKAINSLGAGIIEKIALQFPYRFWDSKVQGADFFGHVPP
SASKRGLFAVFYDMDPQKKHSVLMSVIAGEAVASVRTLDDKQVLQQCMATLRELFKEQEV
PDPTKYFVTRWSTDPWIQMAYSFVKTGGSGEAYDIIAEDIQGTVFFAGEATNRHFPQTVT
GAYLSGVREASKIAAF

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn6
FADFlavin-adenine dinucleotideC27 H33 N9 O15 P22
PO4Phosphate ionO4 P1

Water and common crystallization additives (K) are not listed.

Primary citation

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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