Iron in PDB 9d86: Crystal Structure of Epoxyqueuosine Reductase Queh C9S Mutant From Thermotoga Maritima

All present enzymatic activity of Crystal Structure of Epoxyqueuosine Reductase Queh C9S Mutant From Thermotoga Maritima:
1.17.99.6;

The structure of Crystal Structure of Epoxyqueuosine Reductase Queh C9S Mutant From Thermotoga Maritima, PDB code: 9d86 was solved by Y.Hu, S.D.Bruner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.15 / 1.88
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	52.742, 104.97, 73.678, 90, 90, 90
R / Rfree (%)	20.6 / 25.3

The binding sites of Iron atom in the Crystal Structure of Epoxyqueuosine Reductase Queh C9S Mutant From Thermotoga Maritima (pdb code 9d86). 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 Epoxyqueuosine Reductase Queh C9S Mutant From Thermotoga Maritima, PDB code: 9d86:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Epoxyqueuosine Reductase Queh C9S Mutant From Thermotoga Maritima


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 Epoxyqueuosine Reductase Queh C9S Mutant From Thermotoga Maritima within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:38.2 occ:1.00 FE1 A:SF4201 0.0 38.2 1.0 SG A:CYS169 2.3 41.3 1.0 S2 A:SF4201 2.3 34.9 1.0 S4 A:SF4201 2.3 38.4 1.0 S3 A:SF4201 2.3 42.0 1.0 FE3 A:SF4201 2.7 35.2 1.0 FE4 A:SF4201 2.7 36.7 1.0 FE2 A:SF4201 2.7 40.2 1.0 CB A:CYS169 3.2 39.9 1.0 S1 A:SF4201 3.9 40.8 1.0 CA A:CYS169 4.4 39.1 1.0 C A:CYS169 4.5 35.3 1.0 CE A:LYS120 4.5 57.7 1.0 NZ A:LYS120 4.5 62.7 1.0 SG A:CYS171 4.6 40.2 1.0 N A:GLY170 4.7 36.9 1.0 SG A:CYS87 4.7 46.2 1.0 SG A:CYS90 4.8 34.1 1.0 OE2 A:GLU82 4.8 66.6 1.0 O A:CYS169 4.8 33.9 1.0 ND2 A:ASN32 4.9 34.2 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Epoxyqueuosine Reductase Queh C9S Mutant From Thermotoga Maritima


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 Epoxyqueuosine Reductase Queh C9S Mutant From Thermotoga Maritima within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:40.2 occ:1.00 FE2 A:SF4201 0.0 40.2 1.0 S3 A:SF4201 2.3 42.0 1.0 S1 A:SF4201 2.3 40.8 1.0 S4 A:SF4201 2.3 38.4 1.0 SG A:CYS87 2.3 46.2 1.0 FE3 A:SF4201 2.7 35.2 1.0 FE1 A:SF4201 2.7 38.2 1.0 FE4 A:SF4201 2.7 36.7 1.0 CB A:CYS87 3.3 44.6 1.0 CA A:CYS87 3.6 44.0 1.0 S2 A:SF4201 3.9 34.9 1.0 N A:CYS87 4.2 41.9 1.0 NE A:ARG86 4.3 62.1 1.0 NH2 A:ARG86 4.4 63.7 1.0 CG A:GLU82 4.6 71.7 1.0 CB A:CYS90 4.6 41.4 1.0 SG A:CYS90 4.7 34.1 1.0 SG A:CYS169 4.7 41.3 1.0 SG A:CYS171 4.8 40.2 1.0 CZ A:ARG86 4.8 62.4 1.0 C A:CYS87 4.9 42.7 1.0 C A:ARG86 4.9 43.9 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Epoxyqueuosine Reductase Queh C9S Mutant From Thermotoga Maritima


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 Epoxyqueuosine Reductase Queh C9S Mutant From Thermotoga Maritima within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:35.2 occ:1.00 FE3 A:SF4201 0.0 35.2 1.0 SG A:CYS90 2.3 34.1 1.0 S1 A:SF4201 2.3 40.8 1.0 S4 A:SF4201 2.3 38.4 1.0 S2 A:SF4201 2.3 34.9 1.0 FE1 A:SF4201 2.7 38.2 1.0 FE2 A:SF4201 2.7 40.2 1.0 FE4 A:SF4201 2.7 36.7 1.0 CB A:CYS90 3.1 41.4 1.0 S3 A:SF4201 3.8 42.0 1.0 ND2 A:ASN32 4.4 34.2 1.0 CZ2 A:TRP70 4.6 41.8 1.0 CA A:CYS90 4.6 35.5 1.0 CB A:ASN32 4.6 32.4 1.0 CA A:CYS87 4.7 44.0 1.0 SG A:CYS171 4.7 40.2 1.0 NE1 A:TRP70 4.8 41.3 1.0 SG A:CYS87 4.8 46.2 1.0 SG A:CYS169 4.8 41.3 1.0 CB A:CYS171 4.9 36.2 1.0 CG A:ASN32 5.0 33.1 1.0 CB A:CYS87 5.0 44.6 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Epoxyqueuosine Reductase Queh C9S Mutant From Thermotoga Maritima


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 Epoxyqueuosine Reductase Queh C9S Mutant From Thermotoga Maritima within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:36.7 occ:1.00 FE4 A:SF4201 0.0 36.7 1.0 SG A:CYS171 2.3 40.2 1.0 S3 A:SF4201 2.3 42.0 1.0 S1 A:SF4201 2.3 40.8 1.0 S2 A:SF4201 2.3 34.9 1.0 FE3 A:SF4201 2.7 35.2 1.0 FE1 A:SF4201 2.7 38.2 1.0 FE2 A:SF4201 2.7 40.2 1.0 CB A:CYS171 3.2 36.2 1.0 S4 A:SF4201 3.9 38.4 1.0 N A:CYS171 4.1 34.0 1.0 CA A:CYS171 4.3 36.2 1.0 NE A:ARG86 4.5 62.1 1.0 NH2 A:ARG86 4.5 63.7 1.0 CB A:SER174 4.5 40.6 1.0 OG A:SER174 4.7 34.9 1.0 CZ2 A:TRP70 4.7 41.8 1.0 SG A:CYS169 4.7 41.3 1.0 SG A:CYS90 4.7 34.1 1.0 CB A:CYS169 4.8 39.9 1.0 CZ A:ARG86 4.8 62.4 1.0 N A:SER174 4.9 39.5 1.0 SG A:CYS87 4.9 46.2 1.0

Y.Hu, M.Jaroch, G.Sun, P.C.Dedon, V.De Crecy-Lagard, S.D.Bruner. Mechanism of Catalysis and Substrate Binding of Epoxyqueuosine Reductase in the Biosynthetic Pathway to Queuosine-Modified Trna. Biochemistry 2024.
ISSN: ISSN 0006-2960
PubMed: 39644232
DOI: 10.1021/ACS.BIOCHEM.4C00524