Iron in PDB 7eqk: 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: 7eqk 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)	28.96 / 2.04
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	66.782, 66.782, 116.336, 90, 90, 120
R / Rfree (%)	19.9 / 24.5

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 7eqk). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 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: 7eqk:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 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:Fe201 b:55.7 occ:1.00 OE1 A:GLU70 2.1 39.3 1.0 O11 A:GOA202 2.2 33.6 1.0 NE2 A:HIS109 2.2 33.0 1.0 NE2 A:HIS64 2.3 32.3 1.0 O2 A:GOA202 2.5 43.2 1.0 NE2 A:HIS66 2.5 35.1 1.0 C1 A:GOA202 3.0 56.5 1.0 CD A:GLU70 3.0 38.3 1.0 CD2 A:HIS64 3.1 34.0 1.0 CE1 A:HIS109 3.1 32.1 1.0 CD2 A:HIS109 3.2 32.3 1.0 C2 A:GOA202 3.2 55.3 1.0 OE2 A:GLU70 3.3 37.8 1.0 CD2 A:HIS66 3.4 34.6 1.0 CE1 A:HIS64 3.4 35.3 1.0 CE1 A:HIS66 3.5 33.6 1.0 OH A:TYR72 3.9 33.2 1.0 ND1 A:HIS109 4.2 31.6 1.0 O12 A:GOA202 4.2 39.2 1.0 CG A:HIS109 4.2 33.3 1.0 CG A:HIS64 4.3 35.2 1.0 CG A:GLU70 4.4 33.0 1.0 ND1 A:HIS64 4.4 34.3 1.0 CG A:HIS66 4.5 35.5 1.0 CZ A:TYR72 4.5 29.6 1.0 ND1 A:HIS66 4.5 35.3 1.0 CB A:GLU70 4.7 28.7 1.0 CE1 A:HIS27 4.7 32.6 1.0 CE1 A:TYR72 4.7 31.4 1.0

Iron binding site 2 out of 2 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 B:Fe201 b:38.6 occ:1.00 OE1 B:GLU70 2.1 27.1 1.0 NE2 B:HIS109 2.2 31.6 1.0 O05 B:JAX202 2.3 34.9 1.0 NE2 B:HIS66 2.3 33.7 1.0 NE2 B:HIS64 2.4 36.3 1.0 O01 B:JAX202 2.6 41.0 1.0 CD B:GLU70 3.0 33.4 1.0 CE1 B:HIS109 3.1 30.5 1.0 CD2 B:HIS66 3.1 31.8 1.0 C03 B:JAX202 3.1 42.9 1.0 CD2 B:HIS64 3.2 38.2 1.0 CD2 B:HIS109 3.2 29.6 1.0 C02 B:JAX202 3.3 40.4 1.0 OE2 B:GLU70 3.3 33.1 1.0 CE1 B:HIS64 3.4 40.6 1.0 CE1 B:HIS66 3.4 33.1 1.0 OH B:TYR72 3.9 30.9 1.0 ND1 B:HIS109 4.2 29.6 1.0 O04 B:JAX202 4.3 40.5 1.0 CG B:HIS109 4.3 28.1 1.0 CG B:HIS64 4.3 39.8 1.0 CG B:HIS66 4.3 33.8 1.0 ND1 B:HIS64 4.4 41.6 1.0 CG B:GLU70 4.4 26.1 1.0 ND1 B:HIS66 4.4 33.8 1.0 NE2 B:HIS27 4.5 59.3 1.0 C06 B:JAX202 4.5 43.7 1.0 CZ B:TYR72 4.6 29.6 1.0 CB B:GLU70 4.7 30.8 1.0 CE1 B:TYR72 4.8 28.5 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