Magnesium in PDB 2q3w: Ensemble Refinement of the Protein Crystal Structure of the CYS84ALA CYS85ALA Double Mutant of the [2FE-2S] Ferredoxin Subunit of Toluene- 4-Monooxygenase From Pseudomonas Mendocina KR1

The structure of Ensemble Refinement of the Protein Crystal Structure of the CYS84ALA CYS85ALA Double Mutant of the [2FE-2S] Ferredoxin Subunit of Toluene- 4-Monooxygenase From Pseudomonas Mendocina KR1, PDB code: 2q3w was solved by E.J.Levin, D.A.Kondrashov, G.E.Wesenberg, G.N.Phillips Jr., Center Foreukaryotic Structural Genomics (Cesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.43 / 1.48
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	44.510, 52.400, 83.556, 90.00, 90.00, 90.00
R / Rfree (%)	14.4 / 18.1

The structure of Ensemble Refinement of the Protein Crystal Structure of the CYS84ALA CYS85ALA Double Mutant of the [2FE-2S] Ferredoxin Subunit of Toluene- 4-Monooxygenase From Pseudomonas Mendocina KR1 also contains other interesting chemical elements:

Iron

(Fe)

16 atoms

The binding sites of Magnesium atom in the Ensemble Refinement of the Protein Crystal Structure of the CYS84ALA CYS85ALA Double Mutant of the [2FE-2S] Ferredoxin Subunit of Toluene- 4-Monooxygenase From Pseudomonas Mendocina KR1 (pdb code 2q3w). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Ensemble Refinement of the Protein Crystal Structure of the CYS84ALA CYS85ALA Double Mutant of the [2FE-2S] Ferredoxin Subunit of Toluene- 4-Monooxygenase From Pseudomonas Mendocina KR1, PDB code: 2q3w:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Ensemble Refinement of the Protein Crystal Structure of the CYS84ALA CYS85ALA Double Mutant of the [2FE-2S] Ferredoxin Subunit of Toluene- 4-Monooxygenase From Pseudomonas Mendocina KR1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ensemble Refinement of the Protein Crystal Structure of the CYS84ALA CYS85ALA Double Mutant of the [2FE-2S] Ferredoxin Subunit of Toluene- 4-Monooxygenase From Pseudomonas Mendocina KR1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg901 b:28.0 occ:0.12 O A:SER53 2.2 11.2 0.1 O A:HOH907 2.2 24.4 0.1 O A:HOH904 2.3 33.2 0.1 O A:HOH905 2.3 28.3 0.1 O A:HOH903 2.3 34.8 0.1 O A:HOH906 2.5 30.2 0.1 C A:SER53 3.3 10.9 0.1 CA A:GLU54 3.9 12.2 0.1 N A:GLU54 4.0 11.3 0.1 O A:HOH944 4.1 24.2 0.1 CA A:SER53 4.3 8.8 0.1 O A:GLY55 4.3 12.7 0.1 OG A:SER53 4.4 7.6 0.1 C A:GLU54 4.4 12.8 0.1 CB A:SER53 4.5 8.8 0.1 O A:HOH1023 4.6 19.9 0.1 O A:HOH1005 4.7 42.7 0.1 O A:MET17 4.8 8.6 0.1 N A:GLY55 4.9 12.4 0.1 O A:GLU54 4.9 13.2 0.1 CE A:MET17 5.0 10.9 0.1

Magnesium binding site 2 out of 2 in the Ensemble Refinement of the Protein Crystal Structure of the CYS84ALA CYS85ALA Double Mutant of the [2FE-2S] Ferredoxin Subunit of Toluene- 4-Monooxygenase From Pseudomonas Mendocina KR1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Ensemble Refinement of the Protein Crystal Structure of the CYS84ALA CYS85ALA Double Mutant of the [2FE-2S] Ferredoxin Subunit of Toluene- 4-Monooxygenase From Pseudomonas Mendocina KR1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg902 b:12.4 occ:0.12 O A:HOH910 2.1 21.6 0.1 O A:HOH909 2.1 25.4 0.1 OD2 A:ASP96 2.3 6.2 0.1 O A:HOH911 2.4 18.9 0.1 O A:HOH908 2.5 19.4 0.1 OD1 A:ASP97 3.1 15.4 0.1 CG A:ASP97 3.3 11.7 0.1 CG A:ASP96 3.4 12.4 0.1 OD2 A:ASP97 3.4 11.5 0.1 O A:HOH984 3.7 19.4 0.1 OD1 A:ASP96 3.9 15.7 0.1 CB A:ASP97 4.1 9.8 0.1 N A:ASP97 4.2 6.4 0.1 N A:ASP96 4.4 9.2 0.1 CB A:ASP96 4.6 9.2 0.1 C A:ASP96 4.6 9.3 0.1 CA A:ASP97 4.7 8.7 0.1 CA A:ASP96 4.8 9.1 0.1 O A:LYS94 4.9 9.0 0.1 O A:HOH927 4.9 14.1 0.1

E.J.Levin, D.A.Kondrashov, G.E.Wesenberg, G.N.Phillips. Ensemble Refinement of Protein Crystal Structures: Validation and Application. Structure V. 15 1040 2007.
ISSN: ISSN 0969-2126
PubMed: 17850744
DOI: 10.1016/J.STR.2007.06.019