Magnesium in PDB 3wb2: Hcgb From Methanocaldococcus Jannaschii in Complex with the Guanylyl- Pyridinol Product in A Model Reaction of [Fe]-Hydrogenase Cofactor Biosynthesis

The structure of Hcgb From Methanocaldococcus Jannaschii in Complex with the Guanylyl- Pyridinol Product in A Model Reaction of [Fe]-Hydrogenase Cofactor Biosynthesis, PDB code: 3wb2 was solved by T.Fujishiro, U.Ermler, S.Shima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.51 / 2.44
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	115.010, 97.370, 63.540, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 22.6

The binding sites of Magnesium atom in the Hcgb From Methanocaldococcus Jannaschii in Complex with the Guanylyl- Pyridinol Product in A Model Reaction of [Fe]-Hydrogenase Cofactor Biosynthesis (pdb code 3wb2). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Hcgb From Methanocaldococcus Jannaschii in Complex with the Guanylyl- Pyridinol Product in A Model Reaction of [Fe]-Hydrogenase Cofactor Biosynthesis, PDB code: 3wb2:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Hcgb From Methanocaldococcus Jannaschii in Complex with the Guanylyl- Pyridinol Product in A Model Reaction of [Fe]-Hydrogenase Cofactor Biosynthesis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Hcgb From Methanocaldococcus Jannaschii in Complex with the Guanylyl- Pyridinol Product in A Model Reaction of [Fe]-Hydrogenase Cofactor Biosynthesis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg203 b:49.9 occ:1.00 O3B A:GDP204 2.1 45.0 1.0 O A:HOH327 2.2 42.1 1.0 O A:HOH326 2.2 40.6 1.0 O A:HOH334 2.2 56.3 1.0 O A:HOH328 2.2 46.3 1.0 O1A A:GDP204 2.3 39.5 1.0 PB A:GDP204 3.5 45.4 1.0 PA A:GDP204 3.5 41.3 1.0 O3A A:GDP204 3.8 42.6 1.0 OD2 A:ASP77 3.8 47.0 1.0 OG1 A:THR73 4.0 40.1 1.0 NZ A:LYS86 4.2 29.6 1.0 OAF A:YGP202 4.3 37.8 1.0 O1B A:GDP204 4.3 39.3 1.0 CA A:ARG74 4.3 39.9 1.0 O A:HOH335 4.4 52.9 1.0 CE A:LYS86 4.5 27.1 1.0 O2A A:GDP204 4.5 42.6 1.0 O2B A:GDP204 4.5 36.4 1.0 N A:ARG74 4.6 38.2 1.0 O5' A:GDP204 4.7 44.5 1.0 O A:THR73 4.7 38.0 1.0 C5' A:GDP204 4.7 47.0 1.0 CB A:ARG74 4.7 40.5 1.0 C A:THR73 4.8 38.5 1.0 CG A:ASP77 4.8 43.4 1.0 OD1 A:ASP77 4.9 43.1 1.0 CB A:THR73 5.0 39.8 1.0

Magnesium binding site 2 out of 2 in the Hcgb From Methanocaldococcus Jannaschii in Complex with the Guanylyl- Pyridinol Product in A Model Reaction of [Fe]-Hydrogenase Cofactor Biosynthesis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Hcgb From Methanocaldococcus Jannaschii in Complex with the Guanylyl- Pyridinol Product in A Model Reaction of [Fe]-Hydrogenase Cofactor Biosynthesis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg205 b:19.9 occ:1.00 O A:HOH341 2.2 33.1 1.0 O A:HOH342 2.3 39.7 1.0 OE1 A:GLU160 2.4 61.8 1.0 OE2 A:GLU160 2.7 63.6 1.0 CD A:GLU160 2.9 61.7 1.0 O A:GLU160 4.0 84.4 1.0 O A:HIS161 4.4 62.8 1.0 CG A:GLU160 4.4 61.3 1.0 C A:GLU160 4.6 69.7 1.0 CA A:GLU160 4.9 60.7 1.0

T.Fujishiro, H.Tamura, M.Schick, J.Kahnt, X.Xie, U.Ermler, S.Shima. Identification of the Hcgb Enzyme in [Fe]-Hydrogenase-Cofactor Biosynthesis. Angew.Chem.Int.Ed.Engl. V. 52 12555 2013.
ISSN: ISSN 1433-7851
PubMed: 24249552
DOI: 10.1002/ANIE.201306745