Iron in PDB 8imu: Dihydroxyacid Dehydratase (Dhad) Mutant-V497F

All present enzymatic activity of Dihydroxyacid Dehydratase (Dhad) Mutant-V497F:
4.2.1.9;

The structure of Dihydroxyacid Dehydratase (Dhad) Mutant-V497F, PDB code: 8imu was solved by J.Zhou, X.Zang, Y.Tang, Y.Yan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.00 / 1.93
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	135.12, 135.12, 136.44, 90, 90, 90
R / Rfree (%)	18.2 / 20.8

The binding sites of Iron atom in the Dihydroxyacid Dehydratase (Dhad) Mutant-V497F (pdb code 8imu). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Dihydroxyacid Dehydratase (Dhad) Mutant-V497F, PDB code: 8imu:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Dihydroxyacid Dehydratase (Dhad) Mutant-V497F


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Dihydroxyacid Dehydratase (Dhad) Mutant-V497F within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:73.2 occ:0.73 FE1 A:FES601 0.0 73.2 0.7 S1 A:FES601 2.2 42.7 0.7 S2 A:FES601 2.2 29.1 0.7 O A:HOH993 2.8 46.5 1.0 FE2 A:FES601 3.1 46.5 0.7 CE A:LYS141 3.6 38.5 0.8 OD2 A:ASP140 3.8 35.7 0.2 O A:HOH704 4.2 31.9 1.0 CG A:ASP140 4.3 32.2 0.2 N A:ALA99 4.4 30.7 1.0 NZ A:LYS141 4.4 33.1 0.8 CB A:ASP98 4.5 34.5 1.0 CB A:ALA99 4.7 29.1 1.0 CG A:LYS141 4.7 28.5 0.8 OD1 A:ASP140 4.7 32.8 0.2 CD A:LYS141 4.7 35.4 0.8 N A:ASP98 4.9 26.2 1.0 CB A:ASP140 4.9 29.7 0.2 SG A:CYS139 4.9 26.9 0.2 O A:CYS139 5.0 27.0 0.8

Iron binding site 2 out of 4 in the Dihydroxyacid Dehydratase (Dhad) Mutant-V497F


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Dihydroxyacid Dehydratase (Dhad) Mutant-V497F within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:46.5 occ:0.73 FE2 A:FES601 0.0 46.5 0.7 S2 A:FES601 2.2 29.1 0.7 S1 A:FES601 2.3 42.7 0.7 SG A:CYS139 2.3 26.9 0.2 SG A:CYS66 2.4 27.6 0.2 CA A:ASP140 2.7 32.5 0.8 CB A:ASP140 3.0 23.7 0.8 FE1 A:FES601 3.1 73.2 0.7 O A:CYS139 3.2 27.0 0.8 ND2 A:ASN64 3.3 29.5 1.0 N A:ASP140 3.3 25.6 0.8 C A:CYS139 3.6 27.2 0.8 CB A:CYS139 3.7 26.9 0.2 CA A:CYS139 3.9 27.3 0.2 C A:ASP140 3.9 27.8 0.8 CB A:CYS66 4.0 29.1 0.8 SG A:CYS66 4.1 32.1 0.8 CB A:CYS66 4.2 30.0 0.2 O A:HOH993 4.2 46.5 1.0 CG A:ASN64 4.2 36.8 1.0 OD1 A:ASN64 4.3 32.2 1.0 C A:CYS139 4.3 28.1 0.2 N A:ASP140 4.3 28.8 0.2 O A:HOH785 4.4 31.6 1.0 CG A:ASP140 4.5 29.3 0.8 N A:LYS141 4.5 29.9 0.8 O A:ASP140 4.7 29.6 0.8 CB A:ASP140 4.7 29.7 0.2 CG A:ASP140 4.8 32.2 0.2 CG A:LYS141 5.0 28.5 0.8

Iron binding site 3 out of 4 in the Dihydroxyacid Dehydratase (Dhad) Mutant-V497F


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Dihydroxyacid Dehydratase (Dhad) Mutant-V497F within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:65.4 occ:0.70 FE1 B:FES601 0.0 65.4 0.7 S2 B:FES601 2.2 27.3 0.7 S1 B:FES601 2.2 40.0 0.7 O B:HOH985 2.6 48.2 1.0 FE2 B:FES601 3.0 42.9 0.7 CE B:LYS141 3.6 34.0 0.8 O B:HOH961 3.6 43.9 1.0 OD2 B:ASP140 3.8 36.6 0.2 O B:HOH706 4.1 29.4 1.0 CG B:ASP140 4.2 31.4 0.2 NZ B:LYS141 4.4 31.9 0.8 N B:ALA99 4.5 29.6 1.0 CB B:ASP98 4.5 30.7 1.0 CG B:LYS141 4.6 30.4 0.8 OD1 B:ASP140 4.6 32.0 0.2 CD B:LYS141 4.7 31.2 0.8 CB B:ALA99 4.8 28.3 1.0 CB B:ASP140 4.8 29.9 0.2 O B:CYS139 4.8 27.0 0.8 SG B:CYS139 4.9 25.9 0.2 N B:ASP98 4.9 27.1 1.0

Iron binding site 4 out of 4 in the Dihydroxyacid Dehydratase (Dhad) Mutant-V497F


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Dihydroxyacid Dehydratase (Dhad) Mutant-V497F within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:42.9 occ:0.70 FE2 B:FES601 0.0 42.9 0.7 S2 B:FES601 2.2 27.3 0.7 S1 B:FES601 2.3 40.0 0.7 SG B:CYS139 2.3 25.9 0.2 SG B:CYS66 2.4 26.4 0.2 CA B:ASP140 2.7 28.9 0.8 CB B:ASP140 2.9 26.1 0.8 FE1 B:FES601 3.0 65.4 0.7 O B:CYS139 3.2 27.0 0.8 N B:ASP140 3.3 24.4 0.8 ND2 B:ASN64 3.3 30.1 1.0 C B:CYS139 3.6 25.4 0.8 CB B:CYS139 3.7 26.5 0.2 CA B:CYS139 3.8 27.9 0.2 C B:ASP140 3.9 27.5 0.8 CB B:CYS66 4.1 30.0 0.8 O B:HOH985 4.2 48.2 1.0 N B:ASP140 4.2 28.4 0.2 C B:CYS139 4.2 28.3 0.2 CB B:CYS66 4.2 30.0 0.2 O B:HOH777 4.2 28.7 1.0 SG B:CYS66 4.2 33.1 0.8 CG B:ASN64 4.3 33.9 1.0 OD1 B:ASN64 4.3 30.8 1.0 CG B:ASP140 4.4 28.5 0.8 N B:LYS141 4.4 30.4 0.8 CB B:ASP140 4.7 29.9 0.2 O B:ASP140 4.7 29.7 0.8 CG B:ASP140 4.8 31.4 0.2 CG B:LYS141 4.9 30.4 0.8 OD1 B:ASP140 4.9 25.1 0.8 O B:CYS139 5.0 29.7 0.2

J.Zhou, X.Zang, Y.Tang, Y.Yan. Dihydroxyacid Dehydratase (Dhad) Mutant-V497F To Be Published.