Iron in PDB 7euz: Structural and Mechanistic Studies of A Novel Non-Heme Iron Epimerase/Lyase and Its Utilization in Chemoselective Synthesis.

The structure of Structural and Mechanistic Studies of A Novel Non-Heme Iron Epimerase/Lyase and Its Utilization in Chemoselective Synthesis., PDB code: 7euz was solved by T.L.Li, Y.S.Li, M.H.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.06 / 1.91
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	66.834, 66.834, 116.742, 90, 90, 120
R / Rfree (%)	18.9 / 21.7

The binding sites of Iron atom in the Structural and Mechanistic Studies of A Novel Non-Heme Iron Epimerase/Lyase and Its Utilization in Chemoselective Synthesis. (pdb code 7euz). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Structural and Mechanistic Studies of A Novel Non-Heme Iron Epimerase/Lyase and Its Utilization in Chemoselective Synthesis., PDB code: 7euz:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Structural and Mechanistic Studies of A Novel Non-Heme Iron Epimerase/Lyase and Its Utilization in Chemoselective Synthesis.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structural and Mechanistic Studies of A Novel Non-Heme Iron Epimerase/Lyase and Its Utilization in Chemoselective Synthesis. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:37.3 occ:0.50 FE A:FE202 0.0 37.3 0.5 OE1 A:GLU70 2.0 41.8 1.0 NE2 A:HIS109 2.1 34.4 1.0 NE2 A:HIS64 2.3 33.5 1.0 NE2 A:HIS66 2.3 45.2 1.0 FE A:FE202 2.3 47.6 0.5 O A:HOH305 2.4 51.4 1.0 CD A:GLU70 3.0 44.0 1.0 CD2 A:HIS64 3.0 32.8 1.0 CE1 A:HIS109 3.0 34.7 1.0 CD2 A:HIS109 3.1 32.3 1.0 CD2 A:HIS66 3.2 39.4 1.0 OE2 A:GLU70 3.3 45.6 1.0 CE1 A:HIS66 3.3 39.6 1.0 CE1 A:HIS64 3.4 37.9 1.0 OH A:TYR72 4.0 30.9 1.0 ND1 A:HIS109 4.1 32.1 1.0 CG A:HIS109 4.2 30.1 1.0 CG A:HIS64 4.2 34.4 1.0 CG A:GLU70 4.3 35.2 1.0 CG A:HIS66 4.3 39.8 1.0 ND1 A:HIS66 4.4 38.7 1.0 ND1 A:HIS64 4.4 34.0 1.0 O A:HOH357 4.5 38.6 1.0 CB A:GLU70 4.7 28.4 1.0 CZ A:TYR72 4.8 29.1 1.0 CE1 A:HIS27 4.8 36.0 1.0 CE1 A:TYR72 4.9 35.0 1.0

Iron binding site 2 out of 3 in the Structural and Mechanistic Studies of A Novel Non-Heme Iron Epimerase/Lyase and Its Utilization in Chemoselective Synthesis.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structural and Mechanistic Studies of A Novel Non-Heme Iron Epimerase/Lyase and Its Utilization in Chemoselective Synthesis. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:47.6 occ:0.50 FE A:FE202 0.0 47.6 0.5 FE A:FE202 2.3 37.3 0.5 O A:HOH357 2.4 38.6 1.0 O A:HOH305 2.5 51.4 1.0 OH A:TYR72 2.6 30.9 1.0 NE2 A:HIS64 3.0 33.5 1.0 OE1 A:GLU70 3.1 41.8 1.0 CZ A:TYR72 3.3 29.1 1.0 CE1 A:TYR72 3.3 35.0 1.0 CE1 A:HIS64 3.4 37.9 1.0 OE2 A:GLU70 3.4 45.6 1.0 CD A:GLU70 3.6 44.0 1.0 NE2 A:HIS109 3.6 34.4 1.0 O A:HOH356 3.6 33.1 1.0 CD2 A:HIS109 3.8 32.3 1.0 O1 A:PO3201 3.8 69.4 1.0 CD2 A:HIS64 4.3 32.8 1.0 NE2 A:HIS27 4.4 29.9 1.0 NE2 A:HIS66 4.4 45.2 1.0 CE1 A:HIS27 4.5 36.0 1.0 CE2 A:TYR72 4.6 31.7 1.0 O3 A:PO3201 4.6 59.5 1.0 CD1 A:TYR72 4.7 33.5 1.0 P A:PO3201 4.7 86.8 1.0 ND1 A:HIS64 4.7 34.0 1.0 CE1 A:HIS109 4.8 34.7 1.0 CD1 A:PHE111 4.9 31.1 1.0 O2 A:PO3201 4.9 66.0 1.0

Iron binding site 3 out of 3 in the Structural and Mechanistic Studies of A Novel Non-Heme Iron Epimerase/Lyase and Its Utilization in Chemoselective Synthesis.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structural and Mechanistic Studies of A Novel Non-Heme Iron Epimerase/Lyase and Its Utilization in Chemoselective Synthesis. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:38.9 occ:1.00 OE1 B:GLU70 2.0 28.1 1.0 NE2 B:HIS64 2.2 41.6 1.0 NE2 B:HIS109 2.3 33.8 1.0 NE2 B:HIS66 2.3 36.4 1.0 O01 B:JD3202 2.4 39.2 1.0 N05 B:JD3202 2.4 44.5 1.0 CD B:GLU70 2.9 35.7 1.0 CD2 B:HIS64 3.0 43.7 1.0 CD2 B:HIS66 3.1 38.9 1.0 C02 B:JD3202 3.1 42.2 1.0 CE1 B:HIS109 3.2 34.7 1.0 OE2 B:GLU70 3.2 38.0 1.0 CD2 B:HIS109 3.2 32.1 1.0 C04 B:JD3202 3.3 50.2 1.0 CE1 B:HIS66 3.4 39.3 1.0 CE1 B:HIS64 3.4 48.8 1.0 OH B:TYR72 4.0 31.8 1.0 CG B:HIS64 4.2 45.4 1.0 NE2 B:HIS27 4.2 75.5 1.0 ND1 B:HIS109 4.3 31.3 1.0 O03 B:JD3202 4.3 45.3 1.0 CG B:HIS66 4.3 38.0 1.0 CG B:GLU70 4.3 29.4 1.0 CG B:HIS109 4.3 31.3 1.0 ND1 B:HIS64 4.4 46.1 1.0 ND1 B:HIS66 4.4 41.2 1.0 CB B:GLU70 4.7 34.8 1.0 C06 B:JD3202 4.7 57.1 1.0 CZ B:TYR72 4.7 33.9 1.0 CE1 B:HIS27 4.8 77.9 1.0 CE1 B:TYR72 4.8 36.6 1.0

M.H.Chen, Y.S.Li, N.S.Hsu, K.H.Lin, Y.L.Wang, Z.C.Wang, C.F.Chang, J.P.Lin, C.Y.Chang, T.L.Li. Structural and Mechanistic Bases For STNK3 and Its Mutant-Mediated Lewis-Acid-Dependent Epimerization and Retro-Aldol Reactions. Acs Catalysis V. 12 1945 2022.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.1C04790