Magnesium in PDB 1t57: Crystal Structure of the Conserved Protein MTH1675 From Methanobacterium Thermoautotrophicum

The structure of Crystal Structure of the Conserved Protein MTH1675 From Methanobacterium Thermoautotrophicum, PDB code: 1t57 was solved by Y.Kim, A.Joachimiak, V.Saridakis, X.Xu, C.H.Arrowsmith, D.Christendat, A.Edwards, Midwest Center For Structural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.92 / 2.30
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	103.983, 69.398, 90.953, 90.00, 90.00, 90.00
R / Rfree (%)	25.2 / 31.8

The binding sites of Magnesium atom in the Crystal Structure of the Conserved Protein MTH1675 From Methanobacterium Thermoautotrophicum (pdb code 1t57). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the Conserved Protein MTH1675 From Methanobacterium Thermoautotrophicum, PDB code: 1t57:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of the Conserved Protein MTH1675 From Methanobacterium Thermoautotrophicum


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Conserved Protein MTH1675 From Methanobacterium Thermoautotrophicum within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:46.9 occ:1.00 O A:VAL122 2.5 19.1 1.0 O A:PRO184 2.6 35.8 1.0 OXT A:PRO186 2.6 50.9 1.0 O B:ILE177 2.7 28.6 1.0 O A:ARG185 2.8 34.0 1.0 C A:ARG185 3.1 36.8 1.0 C A:PRO186 3.1 48.1 1.0 O A:PRO186 3.6 47.2 1.0 N A:PRO186 3.6 41.9 1.0 C A:PRO184 3.6 37.8 1.0 C A:VAL122 3.7 20.3 1.0 CA A:ARG185 3.7 32.9 1.0 C B:ILE177 3.8 30.6 1.0 CA A:PRO186 3.9 46.5 1.0 NH2 B:ARG176 4.0 18.8 1.0 N A:ARG185 4.1 36.4 1.0 O A:HOH316 4.2 35.6 1.0 CA B:HIS178 4.3 27.9 1.0 CA A:VAL122 4.4 21.5 1.0 N B:HIS178 4.5 36.6 1.0 CB A:SER123 4.6 22.2 1.0 O B:HIS178 4.7 30.1 1.0 N A:SER123 4.7 18.9 1.0 CD A:PRO186 4.7 43.8 1.0 ND1 B:HIS178 4.7 26.5 1.0 N B:ILE177 4.7 27.0 1.0 CZ B:ARG176 4.8 18.1 1.0 CA A:SER123 4.8 24.6 1.0 O A:MSE121 4.8 35.6 1.0 NE B:ARG176 4.9 22.6 1.0 CA B:ILE177 4.9 28.7 1.0 C B:HIS178 4.9 28.3 1.0 CG1 A:VAL122 4.9 16.4 1.0 CA A:PRO184 4.9 36.1 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of the Conserved Protein MTH1675 From Methanobacterium Thermoautotrophicum


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Conserved Protein MTH1675 From Methanobacterium Thermoautotrophicum within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:52.1 occ:1.00 O2P B:FMN201 2.5 64.3 1.0 OE1 B:GLU43 2.6 0.5 1.0 P B:FMN201 3.6 62.4 1.0 N B:GLY157 3.6 55.0 1.0 CB B:TRP156 3.8 70.5 1.0 CD B:LYS13 3.8 70.3 1.0 CD B:GLU43 3.8 94.5 1.0 O3P B:FMN201 4.0 70.1 1.0 CA B:GLY157 4.1 54.4 1.0 O1P B:FMN201 4.2 68.3 1.0 C B:TRP156 4.2 60.8 1.0 CB B:GLU43 4.3 69.7 1.0 CA B:TRP156 4.4 64.1 1.0 CE B:LYS13 4.5 72.0 1.0 CG B:LYS13 4.6 67.7 1.0 OE2 B:GLU43 4.6 98.3 1.0 CG B:GLU43 4.6 84.8 1.0 CG B:TRP156 4.9 80.2 1.0 O5' B:FMN201 5.0 71.7 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of the Conserved Protein MTH1675 From Methanobacterium Thermoautotrophicum


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the Conserved Protein MTH1675 From Methanobacterium Thermoautotrophicum within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg303 b:71.6 occ:1.00 O B:VAL122 2.3 27.6 1.0 O B:ARG185 2.5 39.7 1.0 OXT B:PRO186 2.6 39.2 1.0 O B:PRO184 2.6 37.7 1.0 O A:ILE177 2.6 28.2 1.0 C B:PRO186 2.9 43.2 1.0 O A:HOH362 2.9 34.5 1.0 C B:ARG185 3.1 37.6 1.0 O B:PRO186 3.2 46.3 1.0 C B:VAL122 3.5 30.1 1.0 N B:PRO186 3.7 42.5 1.0 C B:PRO184 3.7 37.8 1.0 C A:ILE177 3.8 29.7 1.0 NH2 A:ARG176 3.8 20.0 1.0 CA B:PRO186 3.8 42.5 1.0 CA B:ARG185 3.9 32.6 1.0 N B:ARG185 4.2 31.9 1.0 CA B:VAL122 4.3 34.0 1.0 CA A:HIS178 4.3 36.4 1.0 N B:SER123 4.5 28.3 1.0 N A:HIS178 4.5 29.8 1.0 O B:HOH308 4.6 35.3 1.0 CB B:SER123 4.6 30.0 1.0 CA B:SER123 4.7 27.6 1.0 CD2 A:HIS178 4.7 38.0 1.0 CZ A:ARG176 4.7 22.0 1.0 O A:HIS178 4.7 35.0 1.0 N A:ILE177 4.7 26.8 1.0 CA A:ILE177 4.8 33.3 1.0 NE A:ARG176 4.8 17.8 1.0 O B:MSE121 4.9 38.0 1.0 CA B:PRO184 4.9 37.8 1.0 CD B:PRO186 4.9 40.8 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of the Conserved Protein MTH1675 From Methanobacterium Thermoautotrophicum


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of the Conserved Protein MTH1675 From Methanobacterium Thermoautotrophicum within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg304 b:75.9 occ:1.00 O C:PRO184 2.6 90.6 1.0 O C:ARG185 2.7 89.6 1.0 CG1 C:VAL122 3.0 62.0 1.0 SE C:MSE183 3.3 93.5 1.0 O C:VAL122 3.5 85.9 1.0 C C:ARG185 3.5 92.7 1.0 O C:PRO186 3.5 94.0 1.0 C C:PRO184 3.7 87.8 1.0 CA C:ARG185 3.8 96.0 1.0 C C:VAL122 4.0 82.7 1.0 CA C:VAL122 4.2 77.1 1.0 C C:PRO186 4.2 92.6 1.0 CG C:MSE183 4.2 90.8 1.0 CB C:VAL122 4.2 69.5 1.0 N C:ARG185 4.3 90.8 1.0 N C:PRO186 4.6 87.4 1.0 CB C:MSE183 4.7 94.1 1.0 OXT C:PRO186 4.7 97.0 1.0 CB C:SER123 4.8 85.0 1.0 N C:SER123 4.8 83.5 1.0 N C:PRO184 4.9 78.3 1.0 CA C:PRO184 4.9 82.3 1.0 CA C:PRO186 5.0 89.6 1.0

Y.Kim, A.Joachimiak, V.Saridakis, X.Xu, C.H.Arrowsmith, D.Christendat, A.Edwards. Crystal Structure of the Conserved Protein MTH1675 From Methanobacterium Thermoautotrophicum To Be Published.