Iron in PDB 4wq9: Thiosulfate Dehydrogenase (Tsda) From Allochromatium Vinosum - Dithionite Soak

All present enzymatic activity of Thiosulfate Dehydrogenase (Tsda) From Allochromatium Vinosum - Dithionite Soak:
1.8.2.2;

The structure of Thiosulfate Dehydrogenase (Tsda) From Allochromatium Vinosum - Dithionite Soak, PDB code: 4wq9 was solved by J.A.Brito, K.Denkmann, I.A.C.Pereira, C.Dahl, M.Archer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.96 / 1.47
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	79.289, 69.864, 57.805, 90.00, 129.42, 90.00
R / Rfree (%)	14 / 17.9

The structure of Thiosulfate Dehydrogenase (Tsda) From Allochromatium Vinosum - Dithionite Soak also contains other interesting chemical elements:

Iodine

(I)

2 atoms

The binding sites of Iron atom in the Thiosulfate Dehydrogenase (Tsda) From Allochromatium Vinosum - Dithionite Soak (pdb code 4wq9). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Thiosulfate Dehydrogenase (Tsda) From Allochromatium Vinosum - Dithionite Soak, PDB code: 4wq9:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Thiosulfate Dehydrogenase (Tsda) From Allochromatium Vinosum - Dithionite Soak


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Thiosulfate Dehydrogenase (Tsda) From Allochromatium Vinosum - Dithionite Soak within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1001 b:10.2 occ:1.00 FE A:HEC1001 0.0 10.2 1.0 NB A:HEC1001 2.0 9.2 1.0 NA A:HEC1001 2.1 8.8 1.0 NC A:HEC1001 2.1 8.8 1.0 NE2 A:HIS53 2.1 9.7 1.0 ND A:HEC1001 2.1 8.6 1.0 S A:H2S1006 2.2 17.1 0.8 CE1 A:HIS53 2.9 9.9 1.0 C1A A:HEC1001 3.0 9.8 1.0 C1C A:HEC1001 3.0 8.6 1.0 C1B A:HEC1001 3.0 10.3 1.0 C4A A:HEC1001 3.0 11.0 1.0 C4B A:HEC1001 3.0 9.2 1.0 C1D A:HEC1001 3.0 10.3 1.0 C4C A:HEC1001 3.1 8.7 1.0 C4D A:HEC1001 3.1 10.9 1.0 CD2 A:HIS53 3.2 9.0 1.0 CHC A:HEC1001 3.5 10.2 1.0 CHA A:HEC1001 3.5 11.4 1.0 CHB A:HEC1001 3.5 13.0 1.0 CHD A:HEC1001 3.5 10.3 1.0 SG A:CYS96 3.7 21.5 0.4 SG A:CYS96 3.9 17.1 0.6 CB A:CYS96 4.0 13.6 0.6 ND1 A:HIS53 4.1 10.7 1.0 CB A:CYS96 4.2 16.6 0.4 CG A:HIS53 4.2 8.6 1.0 C3A A:HEC1001 4.3 11.0 1.0 C2A A:HEC1001 4.3 10.4 1.0 C2C A:HEC1001 4.3 10.2 1.0 C2B A:HEC1001 4.3 11.3 1.0 C2D A:HEC1001 4.3 12.2 1.0 C3B A:HEC1001 4.3 11.5 1.0 C3C A:HEC1001 4.4 10.0 1.0 C3D A:HEC1001 4.4 13.6 1.0 OD1 A:CYS96 4.4 16.3 0.6 OD2 A:CYS96 4.9 17.5 0.6 S2 A:THJ1007 5.0 25.2 0.4

Iron binding site 2 out of 2 in the Thiosulfate Dehydrogenase (Tsda) From Allochromatium Vinosum - Dithionite Soak


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Thiosulfate Dehydrogenase (Tsda) From Allochromatium Vinosum - Dithionite Soak within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1002 b:9.6 occ:1.00 FE A:HEC1002 0.0 9.6 1.0 NE2 A:HIS164 2.0 8.4 1.0 NB A:HEC1002 2.1 8.1 1.0 NA A:HEC1002 2.1 7.4 1.0 NC A:HEC1002 2.1 7.6 1.0 ND A:HEC1002 2.1 8.4 1.0 SD A:MET209 2.3 10.8 1.0 CD2 A:HIS164 3.0 8.6 1.0 C4B A:HEC1002 3.0 9.1 1.0 C4C A:HEC1002 3.0 8.2 1.0 C4D A:HEC1002 3.0 8.9 1.0 CE1 A:HIS164 3.0 9.1 1.0 C1B A:HEC1002 3.0 8.0 1.0 C4A A:HEC1002 3.0 8.2 1.0 C1A A:HEC1002 3.0 8.5 1.0 C1D A:HEC1002 3.1 9.9 1.0 C1C A:HEC1002 3.1 9.3 1.0 CG A:MET209 3.4 9.6 1.0 CE A:MET209 3.4 12.2 1.0 CHA A:HEC1002 3.5 10.3 1.0 CHD A:HEC1002 3.5 10.8 1.0 CHB A:HEC1002 3.5 8.6 1.0 CHC A:HEC1002 3.5 10.8 1.0 ND1 A:HIS164 4.1 8.4 1.0 CG A:HIS164 4.2 7.9 1.0 CB A:MET209 4.3 12.4 1.0 C3B A:HEC1002 4.3 9.5 1.0 C3D A:HEC1002 4.3 10.7 1.0 C2A A:HEC1002 4.3 8.5 1.0 C2C A:HEC1002 4.3 10.1 1.0 C2B A:HEC1002 4.3 10.6 1.0 C3C A:HEC1002 4.3 10.1 1.0 C2D A:HEC1002 4.3 11.6 1.0 C3A A:HEC1002 4.3 9.8 1.0

J.A.Brito, K.Denkmann, I.A.C.Pereira, C.Dahl, M.Archer. Thiosulfate Dehydrogenase (Tsda) From Allochromatium Vinosum: Structural and Functional Insights Into Thiosulfate Oxidation J.Biol.Chem. 2015.
ISSN: ESSN 1083-351X
DOI: 10.1074/JBC.M114.623397