Iron in PDB 4e4h: Crystal Structure of Histone Demethylase NO66

All present enzymatic activity of Crystal Structure of Histone Demethylase NO66:
1.14.11.27;

The structure of Crystal Structure of Histone Demethylase NO66, PDB code: 4e4h was solved by M.Wu, Y.Tao, J.Zang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.28
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	89.352, 89.352, 304.863, 90.00, 90.00, 120.00
R / Rfree (%)	20.2 / 25.2

The binding sites of Iron atom in the Crystal Structure of Histone Demethylase NO66 (pdb code 4e4h). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Histone Demethylase NO66, PDB code: 4e4h:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Histone Demethylase NO66


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 Histone Demethylase NO66 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1001 b:48.5 occ:1.00 OD2 A:ASP342 2.0 40.4 1.0 NE2 A:HIS405 2.1 36.1 1.0 NE2 A:HIS340 2.2 39.5 1.0 O A:HOH1242 2.4 50.0 1.0 O A:HOH1243 2.4 50.0 1.0 CE1 A:HIS340 2.9 36.5 1.0 CE1 A:HIS405 2.9 35.4 1.0 CG A:ASP342 3.1 38.6 1.0 CD2 A:HIS405 3.2 34.9 1.0 CD2 A:HIS340 3.3 36.1 1.0 OD1 A:ASP342 3.5 42.5 1.0 O A:HOH1203 3.7 39.6 1.0 ND1 A:HIS340 4.0 36.5 1.0 ND1 A:HIS405 4.1 36.5 1.0 CG A:HIS340 4.2 36.2 1.0 CG A:HIS405 4.3 36.2 1.0 CB A:ASP342 4.4 35.5 1.0 O A:HIS340 5.0 35.1 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Histone Demethylase NO66


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 Histone Demethylase NO66 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1001 b:59.6 occ:1.00 NE2 B:HIS340 2.1 39.7 1.0 NE2 B:HIS405 2.1 40.0 1.0 OD2 B:ASP342 2.3 44.8 1.0 O B:HOH1248 2.4 60.0 1.0 O B:HOH1247 2.4 60.0 1.0 CE1 B:HIS340 2.8 38.4 1.0 CD2 B:HIS405 3.1 37.3 1.0 CE1 B:HIS405 3.1 40.1 1.0 CG B:ASP342 3.2 39.6 1.0 CD2 B:HIS340 3.2 38.3 1.0 OD1 B:ASP342 3.4 43.0 1.0 O B:HOH1193 3.9 40.0 1.0 ND1 B:HIS340 3.9 37.6 1.0 CG B:HIS340 4.2 36.6 1.0 ND1 B:HIS405 4.2 40.0 1.0 CG B:HIS405 4.2 39.0 1.0 CB B:ASP342 4.6 35.6 1.0 O B:HIS340 4.9 34.3 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Histone Demethylase NO66


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Histone Demethylase NO66 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe1001 b:48.2 occ:1.00 OD2 C:ASP342 2.1 37.5 1.0 NE2 C:HIS405 2.1 31.5 1.0 O C:HOH1266 2.2 50.0 1.0 NE2 C:HIS340 2.3 41.1 1.0 O C:HOH1267 2.4 50.0 1.0 CE1 C:HIS405 2.9 32.9 1.0 CE1 C:HIS340 3.0 40.6 1.0 CG C:ASP342 3.1 33.1 1.0 CD2 C:HIS405 3.2 31.8 1.0 CD2 C:HIS340 3.3 40.1 1.0 OD1 C:ASP342 3.4 33.2 1.0 O C:HOH1117 3.8 33.8 1.0 ND1 C:HIS405 4.1 33.9 1.0 ND1 C:HIS340 4.1 39.0 1.0 CG C:HIS405 4.3 30.3 1.0 CG C:HIS340 4.3 37.4 1.0 CB C:ASP342 4.4 30.8 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Histone Demethylase NO66


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Histone Demethylase NO66 within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe1001 b:80.8 occ:1.00 O D:HOH1230 2.1 80.0 1.0 NE2 D:HIS405 2.2 38.0 1.0 NE2 D:HIS340 2.3 43.4 1.0 OD2 D:ASP342 2.5 44.6 0.8 CE1 D:HIS405 2.9 38.0 1.0 CE1 D:HIS340 3.0 43.7 1.0 CG D:ASP342 3.3 41.1 0.8 OD1 D:ASP342 3.3 42.3 0.8 CD2 D:HIS340 3.3 42.4 1.0 CD2 D:HIS405 3.4 37.2 1.0 ND1 D:HIS405 4.1 39.8 1.0 ND1 D:HIS340 4.1 43.6 1.0 CG D:HIS340 4.3 41.5 1.0 CG D:HIS405 4.4 38.1 1.0 O D:HOH1184 4.6 38.1 1.0 CB D:ASP342 4.7 39.4 1.0 O D:HIS340 5.0 40.0 1.0

Y.Tao, M.Wu, K.M.Sinha, J.Zang. Tructural Basis For Tetramerization-Dependent Gene Repression By Histone Demethylase NO66 To Be Published.