Cobalt in PDB 8khq: Bifunctional Sulfoxide Synthase OVOA_TH2 in Complex with Histidine and Cysteine

The structure of Bifunctional Sulfoxide Synthase OVOA_TH2 in Complex with Histidine and Cysteine, PDB code: 8khq was solved by J.Wang, K.Ye, X.Y.Wang, W.P.Yan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.70 / 2.69
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	72.262, 119.114, 412.429, 90, 90, 90
R / Rfree (%)	20.1 / 24.3

The binding sites of Cobalt atom in the Bifunctional Sulfoxide Synthase OVOA_TH2 in Complex with Histidine and Cysteine (pdb code 8khq). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 4 binding sites of Cobalt where determined in the Bifunctional Sulfoxide Synthase OVOA_TH2 in Complex with Histidine and Cysteine, PDB code: 8khq:
Jump to Cobalt binding site number: 1; 2; 3; 4;

Cobalt binding site 1 out of 4 in the Bifunctional Sulfoxide Synthase OVOA_TH2 in Complex with Histidine and Cysteine


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Bifunctional Sulfoxide Synthase OVOA_TH2 in Complex with Histidine and Cysteine within 5.0Å range: probe atom residue distance (Å) B Occ A:Co801 b:57.4 occ:1.00 NE2 A:HIS162 2.2 48.6 1.0 SG A:CYS803 2.2 61.8 1.0 O A:HOH940 2.2 69.3 1.0 NE2 A:HIS166 2.3 57.5 1.0 NE2 A:HIS71 2.3 60.4 1.0 NE2 A:HIS802 2.5 58.6 1.0 CE1 A:HIS162 3.0 54.5 1.0 CE1 A:HIS166 3.1 54.9 1.0 CD2 A:HIS71 3.1 52.2 1.0 CD2 A:HIS162 3.2 50.1 1.0 CE1 A:HIS71 3.3 55.7 1.0 CD2 A:HIS166 3.3 48.9 1.0 CD2 A:HIS802 3.4 54.8 1.0 CB A:CYS803 3.4 69.0 1.0 CE1 A:HIS802 3.5 53.8 1.0 ND1 A:HIS162 4.2 51.7 1.0 ND1 A:HIS166 4.3 53.0 1.0 CG A:HIS162 4.3 47.7 1.0 CG A:HIS71 4.3 50.5 1.0 ND1 A:HIS71 4.4 56.4 1.0 CG A:HIS166 4.4 48.6 1.0 CG A:HIS802 4.6 56.1 1.0 ND1 A:HIS802 4.6 57.9 1.0 CA A:CYS803 4.8 76.2 1.0

Cobalt binding site 2 out of 4 in the Bifunctional Sulfoxide Synthase OVOA_TH2 in Complex with Histidine and Cysteine


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Bifunctional Sulfoxide Synthase OVOA_TH2 in Complex with Histidine and Cysteine within 5.0Å range: probe atom residue distance (Å) B Occ B:Co801 b:55.6 occ:1.00 NE2 B:HIS162 2.2 45.6 1.0 NE2 B:HIS166 2.3 49.8 1.0 NE2 B:HIS71 2.3 53.8 1.0 O B:HOH928 2.3 53.2 1.0 NE2 B:HIS802 2.3 72.1 1.0 SG B:CYS803 2.6 72.5 1.0 CE1 B:HIS162 3.0 45.6 1.0 CD2 B:HIS71 3.1 52.0 1.0 CE1 B:HIS166 3.1 47.0 1.0 CD2 B:HIS162 3.3 46.8 1.0 CE1 B:HIS802 3.3 72.1 1.0 CD2 B:HIS802 3.3 72.1 1.0 CD2 B:HIS166 3.3 46.7 1.0 CE1 B:HIS71 3.4 55.9 1.0 CB B:CYS803 3.6 72.2 1.0 ND1 B:HIS162 4.2 50.2 1.0 ND1 B:HIS166 4.3 49.7 1.0 CG B:HIS71 4.3 55.2 1.0 CG B:HIS162 4.3 49.8 1.0 ND1 B:HIS802 4.4 72.0 1.0 CG B:HIS166 4.4 42.2 1.0 ND1 B:HIS71 4.4 56.3 1.0 CG B:HIS802 4.4 72.0 1.0

Cobalt binding site 3 out of 4 in the Bifunctional Sulfoxide Synthase OVOA_TH2 in Complex with Histidine and Cysteine


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 3 of Bifunctional Sulfoxide Synthase OVOA_TH2 in Complex with Histidine and Cysteine within 5.0Å range: probe atom residue distance (Å) B Occ C:Co801 b:61.5 occ:1.00 NE2 C:HIS162 2.2 51.9 1.0 NE2 C:HIS166 2.2 58.5 1.0 NE2 C:HIS71 2.3 60.6 1.0 NE2 C:HIS802 2.4 72.8 1.0 SG C:CYS803 2.6 72.7 1.0 CE1 C:HIS166 3.1 59.3 1.0 CE1 C:HIS162 3.1 57.6 1.0 CD2 C:HIS71 3.1 53.4 1.0 CD2 C:HIS162 3.2 51.5 1.0 CD2 C:HIS166 3.3 54.6 1.0 CD2 C:HIS802 3.3 72.8 1.0 CE1 C:HIS71 3.4 56.6 1.0 CE1 C:HIS802 3.4 72.8 1.0 CB C:CYS803 3.6 72.6 1.0 ND1 C:HIS162 4.2 57.0 1.0 ND1 C:HIS166 4.2 53.6 1.0 CG C:HIS162 4.3 51.5 1.0 CG C:HIS71 4.3 58.4 1.0 CG C:HIS166 4.4 54.7 1.0 ND1 C:HIS71 4.4 62.3 1.0 ND1 C:HIS802 4.5 72.7 1.0 CG C:HIS802 4.5 72.7 1.0 OH C:TYR406 4.9 56.3 1.0

Cobalt binding site 4 out of 4 in the Bifunctional Sulfoxide Synthase OVOA_TH2 in Complex with Histidine and Cysteine


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 4 of Bifunctional Sulfoxide Synthase OVOA_TH2 in Complex with Histidine and Cysteine within 5.0Å range: probe atom residue distance (Å) B Occ D:Co801 b:89.2 occ:1.00 NE2 D:HIS162 2.2 84.4 1.0 SG D:CYS803 2.3 93.6 1.0 NE2 D:HIS71 2.3 90.0 1.0 NE2 D:HIS802 2.3 98.5 1.0 NE2 D:HIS166 2.4 106.1 1.0 CE1 D:HIS162 3.0 87.3 1.0 CE1 D:HIS802 3.0 94.6 1.0 CD2 D:HIS71 3.2 97.9 1.0 CE1 D:HIS71 3.3 93.8 1.0 CD2 D:HIS162 3.3 86.5 1.0 CE1 D:HIS166 3.4 101.9 1.0 CD2 D:HIS166 3.4 95.9 1.0 CD2 D:HIS802 3.5 100.2 1.0 CB D:CYS803 3.7 109.5 1.0 ND1 D:HIS162 4.1 86.8 1.0 ND1 D:HIS802 4.2 93.5 1.0 CG D:HIS162 4.4 83.2 1.0 ND1 D:HIS71 4.4 94.0 1.0 CG D:HIS71 4.4 90.9 1.0 ND1 D:HIS166 4.5 98.8 1.0 CG D:HIS802 4.5 100.6 1.0 CG D:HIS166 4.5 95.6 1.0 OH D:TYR406 4.9 81.5 1.0

X.Wang, S.Hu, J.Wang, T.Zhang, K.Ye, A.Wen, G.Zhu, A.Vegas, L.Zhang, W.Yan, X.Liu, P.Liu. Biochemical and Structural Characterization of OVOATH2: A Mononuclear Nonheme Iron Enzyme From Hydrogenimonas Thermophila For Ovothiol Biosynthesis Acs Catalysis 15417 2023.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.3C04026