Magnesium in PDB 6nxj: Flavin Transferase Apbe From Vibrio Cholerae, H257G Mutant

All present enzymatic activity of Flavin Transferase Apbe From Vibrio Cholerae, H257G Mutant:
2.7.1.180;

The structure of Flavin Transferase Apbe From Vibrio Cholerae, H257G Mutant, PDB code: 6nxj was solved by J.Osipiuk, X.Fang, S.Chakravarthy, O.Juarez, A.Joachimiak, Center Forstructural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.85 / 1.92
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.161, 71.922, 104.569, 90.00, 93.29, 90.00
R / Rfree (%)	19.4 / 23.7

The binding sites of Magnesium atom in the Flavin Transferase Apbe From Vibrio Cholerae, H257G Mutant (pdb code 6nxj). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Flavin Transferase Apbe From Vibrio Cholerae, H257G Mutant, PDB code: 6nxj:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Flavin Transferase Apbe From Vibrio Cholerae, H257G Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Flavin Transferase Apbe From Vibrio Cholerae, H257G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:24.2 occ:1.00 O2A A:FAD500 2.2 19.5 1.0 O A:ASP285 2.3 26.9 1.0 OG1 A:THR289 2.3 24.7 1.0 OD1 A:ASP285 2.3 22.0 1.0 O A:THR171 2.5 26.8 1.0 OG1 A:THR171 2.5 28.7 1.0 C A:ASP285 3.1 24.9 1.0 PA A:FAD500 3.3 23.1 1.0 MG A:MG502 3.3 22.8 1.0 CG A:ASP285 3.3 23.7 1.0 C A:THR171 3.4 26.0 1.0 CB A:THR289 3.4 25.4 1.0 CA A:THR171 3.5 25.4 1.0 CB A:THR171 3.6 26.5 1.0 O5B A:FAD500 3.6 23.6 1.0 O1A A:FAD500 3.7 20.9 1.0 O A:HOH638 3.8 31.4 1.0 CA A:ASP285 3.9 23.3 1.0 O A:HOH615 3.9 21.8 1.0 N A:GLY286 4.0 25.9 1.0 CB A:ASP285 4.1 23.0 1.0 OD2 A:ASP285 4.2 20.8 1.0 CA A:GLY286 4.3 25.6 1.0 OG A:SER241 4.3 33.8 1.0 N A:THR289 4.3 26.6 1.0 CG2 A:THR171 4.4 26.3 1.0 CG2 A:THR289 4.4 26.0 1.0 CA A:THR289 4.5 25.6 1.0 N A:ILE172 4.6 23.9 1.0 O3P A:FAD500 4.7 23.9 1.0 C A:GLY286 4.8 25.4 1.0 O A:GLY286 4.8 25.1 1.0 O2P A:FAD500 4.9 24.6 1.0 N A:THR171 4.9 26.0 1.0

Magnesium binding site 2 out of 4 in the Flavin Transferase Apbe From Vibrio Cholerae, H257G Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Flavin Transferase Apbe From Vibrio Cholerae, H257G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:22.8 occ:1.00 O2P A:FAD500 2.0 24.6 1.0 O2A A:FAD500 2.0 19.5 1.0 O A:HOH615 2.1 21.8 1.0 OD1 A:ASP285 2.1 22.0 1.0 O A:HOH638 2.2 31.4 1.0 OE1 A:GLU200 2.2 32.6 1.0 CG A:ASP285 3.0 23.7 1.0 CD A:GLU200 3.1 29.6 1.0 P A:FAD500 3.2 26.7 1.0 PA A:FAD500 3.2 23.1 1.0 MG A:MG501 3.3 24.2 1.0 OD2 A:ASP285 3.3 20.8 1.0 O3P A:FAD500 3.5 23.9 1.0 OE2 A:GLU200 3.5 29.1 1.0 O5' A:FAD500 3.7 30.9 1.0 O A:HOH757 4.0 35.6 1.0 NZ A:LYS174 4.2 35.8 1.0 O5B A:FAD500 4.2 23.6 1.0 CG A:GLU200 4.2 29.5 1.0 O1A A:FAD500 4.2 20.9 1.0 O A:THR171 4.3 26.8 1.0 CB A:ASP285 4.4 23.0 1.0 CE A:LYS174 4.4 33.1 1.0 O1P A:FAD500 4.5 27.1 1.0 O A:SER170 4.6 24.9 1.0 C A:THR171 4.7 26.0 1.0 CD A:LYS174 4.7 33.1 1.0 O A:ASP285 4.8 26.9 1.0 CA A:THR171 4.8 25.4 1.0 CA A:ASP285 4.8 23.3 1.0 CB A:LYS174 4.9 30.1 1.0 O A:THR240 4.9 27.6 1.0 OG1 A:THR289 4.9 24.7 1.0

Magnesium binding site 3 out of 4 in the Flavin Transferase Apbe From Vibrio Cholerae, H257G Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Flavin Transferase Apbe From Vibrio Cholerae, H257G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:31.6 occ:1.00 O B:ASP285 2.3 31.3 1.0 O B:THR171 2.3 24.7 1.0 OG1 B:THR289 2.3 30.4 1.0 O2A B:FAD500 2.4 30.5 1.0 OG1 B:THR171 2.6 29.5 1.0 OD1 B:ASP285 2.6 30.4 1.0 C B:ASP285 3.0 30.3 1.0 C B:THR171 3.2 27.9 1.0 CB B:THR289 3.4 32.7 1.0 PA B:FAD500 3.4 33.1 1.0 CG B:ASP285 3.4 29.4 1.0 CA B:THR171 3.5 28.3 1.0 MG B:MG502 3.5 30.9 1.0 CB B:THR171 3.6 28.8 1.0 O5B B:FAD500 3.8 32.7 1.0 CA B:ASP285 3.8 29.0 1.0 O B:HOH686 3.8 37.5 1.0 N B:GLY286 3.9 31.9 1.0 O1A B:FAD500 4.0 32.2 1.0 O B:HOH628 4.1 28.4 1.0 CB B:ASP285 4.1 29.2 1.0 CA B:GLY286 4.2 34.3 1.0 N B:THR289 4.2 35.5 1.0 OD2 B:ASP285 4.2 28.8 1.0 OG B:SER241 4.3 37.6 1.0 CG2 B:THR289 4.4 32.1 1.0 CG2 B:THR171 4.4 29.0 1.0 CA B:THR289 4.4 33.9 1.0 N B:ILE172 4.5 29.3 1.0 O B:GLY286 4.6 33.3 1.0 C B:GLY286 4.6 33.6 1.0 O3P B:FAD500 4.9 32.2 1.0 N B:THR171 4.9 27.9 1.0

Magnesium binding site 4 out of 4 in the Flavin Transferase Apbe From Vibrio Cholerae, H257G Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Flavin Transferase Apbe From Vibrio Cholerae, H257G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:30.9 occ:1.00 O2P B:FAD500 2.0 33.5 1.0 O2A B:FAD500 2.0 30.5 1.0 OE1 B:GLU200 2.1 36.5 1.0 O B:HOH628 2.2 28.4 1.0 O B:HOH686 2.2 37.5 1.0 OD1 B:ASP285 2.2 30.4 1.0 CD B:GLU200 3.2 34.9 1.0 P B:FAD500 3.2 32.5 1.0 CG B:ASP285 3.2 29.4 1.0 PA B:FAD500 3.2 33.1 1.0 O3P B:FAD500 3.5 32.2 1.0 MG B:MG501 3.5 31.6 1.0 OD2 B:ASP285 3.6 28.8 1.0 O5' B:FAD500 3.8 33.6 1.0 OE2 B:GLU200 3.8 38.9 1.0 O B:HOH694 3.9 38.7 1.0 NZ B:LYS174 4.1 44.6 1.0 CE B:LYS174 4.1 42.5 1.0 CG B:GLU200 4.2 34.9 1.0 O1A B:FAD500 4.3 32.2 1.0 O5B B:FAD500 4.3 32.7 1.0 O B:THR171 4.4 24.7 1.0 O1P B:FAD500 4.5 35.5 1.0 CB B:ASP285 4.5 29.2 1.0 O B:SER170 4.7 28.8 1.0 C B:THR171 4.8 27.9 1.0 O B:THR240 4.8 32.0 1.0 CA B:THR171 4.9 28.3 1.0 OG1 B:THR289 4.9 30.4 1.0 CA B:ASP285 4.9 29.0 1.0 O B:ASP285 4.9 31.3 1.0 CD B:LYS174 5.0 41.1 1.0

X.Fang, J.Osipiuk, S.Chakravarthy, M.Yuan, W.M.Menzer, D.Nissen, P.Liang, D.A.Raba, K.Tuz, A.J.Howard, A.Joachimiak, D.D.L.Minh, O.Juarez. Conserved Residue His-257 Ofvibrio Choleraeflavin Transferase Apbe Plays A Critical Role in Substrate Binding and Catalysis. J.Biol.Chem. V. 294 13800 2019.
ISSN: ESSN 1083-351X
PubMed: 31350338
DOI: 10.1074/JBC.RA119.008261