Iron in PDB 4tn7: Crystal Structure of Mouse KDM2A-H3K36ME-No Complex

All present enzymatic activity of Crystal Structure of Mouse KDM2A-H3K36ME-No Complex:
1.14.11.27;

The structure of Crystal Structure of Mouse KDM2A-H3K36ME-No Complex, PDB code: 4tn7 was solved by Z.Cheng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.17 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	55.063, 157.928, 48.706, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 27.9

The binding sites of Iron atom in the Crystal Structure of Mouse KDM2A-H3K36ME-No Complex (pdb code 4tn7). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Mouse KDM2A-H3K36ME-No Complex, PDB code: 4tn7:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Mouse KDM2A-H3K36ME-No Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Mouse KDM2A-H3K36ME-No Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:33.4 occ:1.00 N A:NO602 2.1 32.4 1.0 OD1 A:ASP214 2.2 39.0 1.0 NE2 A:HIS212 2.3 23.7 1.0 NE2 A:HIS284 2.3 16.3 1.0 O4 A:SIN603 2.3 35.5 1.0 CG A:ASP214 3.0 36.0 1.0 C4 A:SIN603 3.1 39.4 1.0 OD2 A:ASP214 3.1 43.3 1.0 O A:NO602 3.2 34.7 1.0 CE1 A:HIS284 3.2 16.2 1.0 CE1 A:HIS212 3.2 23.4 1.0 CD2 A:HIS212 3.3 22.0 1.0 CD2 A:HIS284 3.4 16.4 1.0 O3 A:SIN603 3.4 43.5 1.0 H32 A:SIN603 4.3 48.0 1.0 C3 A:SIN603 4.3 40.0 1.0 ND1 A:HIS284 4.3 25.6 1.0 ND1 A:HIS212 4.4 19.8 1.0 CG A:HIS212 4.4 20.4 1.0 CB A:ASP214 4.4 25.8 1.0 CG A:HIS284 4.5 26.6 1.0 CM E:MLZ36 4.5 38.3 1.0 N A:ASP214 4.8 16.0 1.0 H22 A:SIN603 4.9 43.0 1.0 CA A:ASP214 4.9 17.6 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Mouse KDM2A-H3K36ME-No Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Mouse KDM2A-H3K36ME-No Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe601 b:32.9 occ:1.00 OD1 C:ASP214 2.3 40.4 1.0 NE2 C:HIS284 2.3 16.6 1.0 O2 C:SIN602 2.3 33.4 1.0 O1 C:SIN602 2.5 44.6 1.0 NE2 C:HIS212 2.5 23.1 1.0 C1 C:SIN602 2.8 38.4 1.0 OD2 C:ASP214 2.9 44.0 1.0 CG C:ASP214 2.9 39.8 1.0 CE1 C:HIS284 3.2 27.4 1.0 CD2 C:HIS284 3.4 16.6 1.0 CD2 C:HIS212 3.4 22.1 1.0 CE1 C:HIS212 3.5 23.7 1.0 C2 C:SIN602 4.3 37.0 1.0 ND1 C:HIS284 4.3 29.2 1.0 CB C:ASP214 4.4 33.9 1.0 CG C:HIS284 4.5 30.6 1.0 ND1 C:HIS212 4.6 21.7 1.0 CG C:HIS212 4.6 21.5 1.0 CM F:MLZ36 4.6 31.9 1.0 H22 C:SIN602 4.7 44.4 1.0 N C:ASP214 4.8 31.1 1.0 CA C:ASP214 4.8 29.0 1.0 H31 C:SIN602 4.9 43.2 1.0 H21 C:SIN602 4.9 44.4 1.0 H32 C:SIN602 4.9 43.2 1.0 C3 C:SIN602 5.0 36.0 1.0

Z.Cheng, P.Cheung, A.J.Kuo, E.T.Yukl, C.M.Wilmot, O.Gozani, D.J.Patel. A Molecular Threading Mechanism Underlies Jumonji Lysine Demethylase KDM2A Regulation of Methylated H3K36. Genes Dev. V. 28 1758 2014.
ISSN: ISSN 0890-9369
PubMed: 25128496
DOI: 10.1101/GAD.246561.114