1.14.11.67: [histone H3]-trimethyl-L-lysine4 demethylase

This is an abbreviated version!
For detailed information about [histone H3]-trimethyl-L-lysine4 demethylase, go to the full flat file.

Reaction

Synonyms

amine oxidase (flavin-containing) domain 1, AOF1, At2g34880, CG33182, CG33185, CG3654, dJARID2, dJARID2/CG3654, dJMJD2(1), dJMJD2(1)/CG15835, dJMJD2(2), dJMJD2(2)/CG33182, Fbxl10, GH09982, H3K4 demethylase, H3K4 demethylase lysine-specific demethylase 5A, H3K4 histone demethylase, H3K4me3 demethylase, H3K4me3 histone demethylase, H3K4me3-specific demethylase, H3K4me3/2 histone demethylase, H3K9 trimethyl demethylase, histone 3 lysine 4 demethylase, histone demethylase, histone H3 lysine 4 demethylase, histone H3 lysine-4 demethylase, histone H3-K4 demethylase, histone H3K4 demethylase, histone H3K4-specific demethylase, histone lysine demethylase, histone-H3K4-specific demethylase, Jarid1, Jarid1a, JARID1B, JARID1C, Jarid2, JaridB, Jhd2, Jhdm1b/Kdm2b, JMJ15, JMJ703, JmjC domain histone demethylase, JmjC domain-containing histone demethylation protein 3A, JmjC domain-containing histone demethylation protein 3b, JmjC+N, JmjC+N histone demethylase, JMJD2A, JMJD2A-tudor, JMJD2B, jumonji AT rich interactive domain 1B, jumonji AT-rich interactive domain 1B, Jumonji demethylase, KDM1, KDM1B, KDM2, KDM5, KDM5A, KDM5B, KDM5b/JARID1b, KDM5C, KDM5D, Lid, little imaginal discs, LSD1, lysine demethylase, lysine demethylase 5b, lysine demethylase 7, lysine-specific demethylase, lysine-specific demethylase 1, lysine-specific demethylase 5A, lysine-specific demethylase 5B, lysine-specific demethylase JMJ703, Lysine-specific demethylase SE14, More, Ndy1, Os03g0151300, PHD finger protein 8, PHF8, PKDM7B, PLU-1, PLU1, RB-binding protein 2, RBP2, RBR-2, retinoblastoma binding protein 2, SE14, SMCX, trimethylated lysine 4 of histone H3 demethylase

ECTree

     1 Oxidoreductases

         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor

                1.14.11.67 [histone H3]-trimethyl-L-lysine4 demethylase

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Results	in table
6	Activating Compound
5242	AA Sequence
2	Application
32	Cloned(Commentary)
2	Cofactor
6	Crystallization (Commentary)
2154	Disease/ Diagnostics
5	Expression
110	General Information
18	IC50 Value
98	Inhibitors
17	kcat/KM [mM/s]
22	KM Value [mM]
39	Localization
21	Metals/Ions
1	Molecular Weight [Da]
122	Natural Substrates/ Products (Substrates)
245	Organism
2	PDB ID
6	pH Optimum
52	Protein Variants
13	Purification (Commentary)
4	Reaction
74	Reference
110	Source Tissue
169	Substrates and Products (Substrate)
8	Subunits
210	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
20	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.14.11.67 - [histone H3]-trimethyl-L-lysine4 demethylase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

JMJD2A-tudor in complex with H4K20me3, X-ray diffraction structure determination and analysis at 2.8 A resolution

Homo sapiens

O75164

700373

N-terminal fragments of the enzyme in complex with inhibitors, sitting drop vapor diffusion method, using 1.2-1.35 M (NH4)2SO4, 0.1 M Tris-HCl (pH 8.6-9.2), 0-20% (v/v) glycerol and 25 mM (Na/K) dibasic/monobasic phosphate

Homo sapiens

-

757397

purified recombinant enzyme in complex with inhibitor KDOAM-25, sitting drop vapor diffusion method, mixing of 50 nl of 8.1 mg/ml protein in solution with 1 mM KDOAM-25 and 4 mM MnCl2, is mixed with ,precipitant solution consisting of 1.6 M Na/K phosphate, and 0.1 M HEPES, pH 7.5, and 20 nL of KDM5B seeds of crystals obtained from the same condition, 4°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, modeling

Homo sapiens

P29375, P41229, Q9BY66, Q9UGL1

744646

solution strucuture of apo and H3-bound domain PHD1. The H3 peptide adopts a helical conformation that allows for extended interactions between the H3 ligand and PHD1 reader domain. H3 residues A1, R2, and K4 are the major determinants of H3 peptide binding, with smaller contributions from H3T3

Homo sapiens

P29375

763807

structure of intact multi-domain KDM5B. The PLU region, in the central region of KDM5B, has a curved alpha-helical three-dimensional structure that acts as a rigid linker between the catalytic core and a region comprising four alpha-helices, a loop comprising the PHD2 domain, two large intrinsically disordered loops and the PHD3 domain in close proximity. The dumbbell shaped and curved KDM5B architecture is complementary to the nucleosome surface and has a striking overall similarity to that of the functionally related KDM1A/CoREST complex

Homo sapiens

Q9UGL1

765824

purified recombinant enzyme, free or in complex with N-oxalylglycine, X-ray diffraction structure determination and analysis at 2.35 A resolution

Oryza sativa

Q53WJ1

726261