Magnesium in PDB 8g1n: Structure of Campylobacter Concisus Pglc I57M/Q175M Variant with Modeled C-Terminus

All present enzymatic activity of Structure of Campylobacter Concisus Pglc I57M/Q175M Variant with Modeled C-Terminus:
2.7.8.36;

The structure of Structure of Campylobacter Concisus Pglc I57M/Q175M Variant with Modeled C-Terminus, PDB code: 8g1n was solved by G.J.Dodge, L.C.Ray, D.Das, B.Imperiali, K.N.Allen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	62.81 / 2.74
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	70.802, 70.802, 188.442, 90, 90, 120
R / Rfree (%)	25.9 / 29.7

The binding sites of Magnesium atom in the Structure of Campylobacter Concisus Pglc I57M/Q175M Variant with Modeled C-Terminus (pdb code 8g1n). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Campylobacter Concisus Pglc I57M/Q175M Variant with Modeled C-Terminus, PDB code: 8g1n:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Campylobacter Concisus Pglc I57M/Q175M Variant with Modeled C-Terminus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Campylobacter Concisus Pglc I57M/Q175M Variant with Modeled C-Terminus within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:72.3 occ:1.00 O A:ARG88 2.2 71.3 1.0 O3 A:PO4302 2.3 85.9 1.0 OD1 A:ASP93 2.7 55.6 1.0 O2 A:PO4302 2.8 96.1 1.0 C A:ARG88 2.9 59.6 1.0 CA A:ARG88 2.9 54.7 1.0 P A:PO4302 3.0 110.9 1.0 CA A:SER91 3.1 56.0 1.0 N A:SER91 3.4 58.7 1.0 CG A:ASP93 3.5 53.2 1.0 OD2 A:ASP93 3.6 55.9 1.0 CB A:ARG88 3.7 59.0 1.0 O4 A:PO4302 3.7 91.0 1.0 O A:ILE87 3.7 68.3 1.0 OG A:SER91 3.8 70.4 1.0 CB A:SER91 3.9 56.5 1.0 C A:SER91 4.0 53.1 1.0 N A:ARG88 4.1 60.5 1.0 N A:SER89 4.2 56.6 1.0 C A:ILE87 4.3 62.4 1.0 CG A:GLU94 4.3 70.1 1.0 O1 A:PO4302 4.3 103.9 1.0 OE2 A:GLU94 4.3 70.5 1.0 CG A:ARG88 4.4 65.9 1.0 N A:LEU92 4.4 49.1 1.0 C A:LEU90 4.7 63.4 1.0 O A:SER91 4.7 54.0 1.0 N A:ASP93 4.8 53.5 1.0 CD A:GLU94 4.9 71.0 1.0 CB A:ASP93 4.9 59.9 1.0 CA A:SER89 5.0 59.4 1.0 N A:LEU90 5.0 57.8 1.0 C A:SER89 5.0 60.7 1.0

Magnesium binding site 2 out of 2 in the Structure of Campylobacter Concisus Pglc I57M/Q175M Variant with Modeled C-Terminus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Campylobacter Concisus Pglc I57M/Q175M Variant with Modeled C-Terminus within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:80.9 occ:1.00 O B:HOH403 2.1 67.0 1.0 OE2 B:GLU94 2.5 92.3 1.0 OD1 B:ASP93 3.1 72.2 1.0 OD2 B:ASP93 3.4 71.3 1.0 O B:ARG88 3.4 70.7 1.0 CD B:GLU94 3.5 83.0 1.0 CG B:ASP93 3.7 66.9 1.0 CG B:GLU94 4.0 72.6 1.0 CA B:ARG88 4.0 72.8 1.0 C B:ARG88 4.1 72.7 1.0 CB B:ARG88 4.2 71.3 1.0 CA B:SER91 4.5 67.5 1.0 OE1 B:GLU94 4.6 73.6 1.0 CG B:ARG88 4.6 71.6 1.0 NZ B:LYS59 4.7 72.9 1.0

A.J.Anderson, G.J.Dodge, K.N.Allen, B.Imperiali. Co-Conserved Sequence Motifs Are Predictive of Substrate Specificity in A Family of Monotopic Phosphoglycosyl Transferases. Protein Sci. E4646 2023.
ISSN: ESSN 1469-896X
PubMed: 37096962
DOI: 10.1002/PRO.4646