Magnesium in PDB 1jgx: Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Asp

The structure of Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Asp, PDB code: 1jgx was solved by A.Camara-Artigas, C.L.Magee, J.C.Williams, J.P.Allen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.97 / 3.01
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	142.110, 142.110, 187.740, 90.00, 90.00, 120.00
R / Rfree (%)	21.1 / 24.9

The structure of Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Asp also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Magnesium atom in the Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Asp (pdb code 1jgx). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Asp, PDB code: 1jgx:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Asp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Asp within 5.0Å range: probe atom residue distance (Å) B Occ L:Mg850 b:45.3 occ:1.00 MG L:BCL850 0.0 45.3 1.0 ND L:BCL850 2.0 44.9 1.0 NC L:BCL850 2.1 45.0 1.0 NA L:BCL850 2.1 47.0 1.0 NB L:BCL850 2.1 47.1 1.0 NE2 M:HIS182 2.5 46.5 1.0 C1B L:BCL850 3.0 47.9 1.0 C4A L:BCL850 3.0 47.4 1.0 C1C L:BCL850 3.0 44.0 1.0 C4D L:BCL850 3.1 45.4 1.0 C1D L:BCL850 3.1 44.3 1.0 C4C L:BCL850 3.1 44.1 1.0 C4B L:BCL850 3.1 48.6 1.0 C1A L:BCL850 3.2 47.6 1.0 CHB L:BCL850 3.2 47.5 1.0 CHC L:BCL850 3.3 46.7 1.0 CHD L:BCL850 3.5 44.4 1.0 CE1 M:HIS182 3.5 47.7 1.0 CHA L:BCL850 3.5 47.0 1.0 CD2 M:HIS182 3.5 47.6 1.0 C2B L:BCL850 4.2 49.0 1.0 C2D L:BCL850 4.3 44.0 1.0 C3A L:BCL850 4.3 47.7 1.0 C3D L:BCL850 4.3 44.8 1.0 C2C L:BCL850 4.4 41.8 1.0 C3C L:BCL850 4.4 41.7 1.0 C2A L:BCL850 4.4 48.7 1.0 ND1 M:HIS182 4.6 47.1 1.0 C3B L:BCL850 4.6 51.0 1.0 CG M:HIS182 4.7 47.1 1.0 OBB M:BPH854 4.8 50.1 1.0 CE2 L:PHE181 4.8 39.1 1.0 CAA L:BCL850 4.9 52.4 1.0 CBD L:BCL850 5.0 47.4 1.0

Magnesium binding site 2 out of 4 in the Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Asp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Asp within 5.0Å range: probe atom residue distance (Å) B Occ L:Mg851 b:45.6 occ:1.00 MG L:BCL851 0.0 45.6 1.0 ND L:BCL851 2.0 46.0 1.0 NC L:BCL851 2.1 46.9 1.0 NA L:BCL851 2.1 47.0 1.0 NB L:BCL851 2.1 45.6 1.0 NE2 L:HIS173 2.6 30.8 1.0 C4A L:BCL851 3.0 46.7 1.0 C4D L:BCL851 3.1 46.7 1.0 C1B L:BCL851 3.1 45.0 1.0 C1D L:BCL851 3.1 45.9 1.0 C1C L:BCL851 3.1 45.5 1.0 C4C L:BCL851 3.1 45.7 1.0 C4B L:BCL851 3.1 45.5 1.0 C1A L:BCL851 3.2 45.6 1.0 CHB L:BCL851 3.3 45.9 1.0 CHC L:BCL851 3.4 46.0 1.0 CE1 L:HIS173 3.4 31.5 1.0 CHD L:BCL851 3.5 46.1 1.0 CHA L:BCL851 3.5 46.0 1.0 CAB M:BCL852 3.5 54.0 1.0 OBB M:BCL852 3.6 56.6 1.0 CBB M:BCL852 3.6 54.1 1.0 CD2 L:HIS173 3.7 32.7 1.0 C3B M:BCL852 4.3 52.3 1.0 C2D L:BCL851 4.3 45.5 1.0 C2B L:BCL851 4.3 44.7 1.0 C3D L:BCL851 4.3 46.0 1.0 C3A L:BCL851 4.4 45.3 1.0 C3B L:BCL851 4.4 43.9 1.0 C2C L:BCL851 4.4 43.8 1.0 C3C L:BCL851 4.4 44.7 1.0 C2A L:BCL851 4.5 44.4 1.0 ND1 L:HIS173 4.6 32.7 1.0 CG L:HIS173 4.8 33.0 1.0 C4B M:BCL852 5.0 50.0 1.0

Magnesium binding site 3 out of 4 in the Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Asp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Asp within 5.0Å range: probe atom residue distance (Å) B Occ L:Mg853 b:30.4 occ:1.00 MG L:BCL853 0.0 30.4 1.0 ND L:BCL853 2.0 29.2 1.0 NC L:BCL853 2.0 30.9 1.0 NA L:BCL853 2.0 31.1 1.0 NB L:BCL853 2.1 32.1 1.0 NE2 L:HIS153 2.8 49.4 1.0 C4A L:BCL853 3.0 31.8 1.0 C1C L:BCL853 3.1 31.6 1.0 C4D L:BCL853 3.1 30.0 1.0 C1B L:BCL853 3.1 32.5 1.0 C1D L:BCL853 3.1 29.1 1.0 C4C L:BCL853 3.1 31.0 1.0 C4B L:BCL853 3.1 32.7 1.0 C1A L:BCL853 3.2 32.0 1.0 CHB L:BCL853 3.3 31.4 1.0 CHC L:BCL853 3.3 31.9 1.0 CHD L:BCL853 3.5 29.1 1.0 CHA L:BCL853 3.5 32.3 1.0 CD2 L:HIS153 3.7 51.8 1.0 CE1 L:HIS153 3.8 51.0 1.0 C2D L:BCL853 4.3 28.6 1.0 C2B L:BCL853 4.3 33.1 1.0 C3A L:BCL853 4.3 32.6 1.0 C3D L:BCL853 4.3 29.9 1.0 C3C L:BCL853 4.4 32.3 1.0 C2C L:BCL853 4.4 31.4 1.0 C3B L:BCL853 4.4 34.4 1.0 C2A L:BCL853 4.4 32.3 1.0 OBB L:BPH855 4.5 48.1 1.0 CE2 M:TYR210 4.8 41.6 1.0 CAA L:BCL853 4.8 33.1 1.0 CG L:HIS153 4.9 52.3 1.0 ND1 L:HIS153 4.9 52.5 1.0 CBD L:BCL853 5.0 35.7 1.0

Magnesium binding site 4 out of 4 in the Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Asp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Asp within 5.0Å range: probe atom residue distance (Å) B Occ M:Mg852 b:48.9 occ:1.00 MG M:BCL852 0.0 48.9 1.0 ND M:BCL852 2.0 47.5 1.0 NC M:BCL852 2.1 48.5 1.0 NB M:BCL852 2.1 50.7 1.0 NA M:BCL852 2.1 47.5 1.0 NE2 M:HIS202 2.7 36.2 1.0 C4D M:BCL852 3.0 46.3 1.0 C4A M:BCL852 3.0 46.8 1.0 C1B M:BCL852 3.1 51.5 1.0 C1C M:BCL852 3.1 48.4 1.0 C1D M:BCL852 3.1 47.3 1.0 C4B M:BCL852 3.1 50.0 1.0 C4C M:BCL852 3.1 47.0 1.0 C1A M:BCL852 3.2 46.8 1.0 CHB M:BCL852 3.3 49.4 1.0 CHC M:BCL852 3.3 48.7 1.0 CHA M:BCL852 3.5 45.3 1.0 CHD M:BCL852 3.5 46.9 1.0 CE1 M:HIS202 3.6 38.5 1.0 CD2 M:HIS202 3.6 38.3 1.0 CAB L:BCL851 3.7 42.0 1.0 OBB L:BCL851 3.8 41.7 1.0 CBB L:BCL851 3.8 43.3 1.0 C2D M:BCL852 4.3 46.8 1.0 C2B M:BCL852 4.3 51.9 1.0 C3D M:BCL852 4.3 46.5 1.0 C3A M:BCL852 4.4 46.0 1.0 C3B L:BCL851 4.4 43.9 1.0 C3B M:BCL852 4.4 52.3 1.0 C2C M:BCL852 4.4 46.7 1.0 C3C M:BCL852 4.4 46.2 1.0 C2A M:BCL852 4.5 46.0 1.0 ND1 M:HIS202 4.7 38.1 1.0 CG M:HIS202 4.8 38.3 1.0 CBD M:BCL852 5.0 45.0 1.0

A.Camara-Artigas, C.L.Magee, J.C.Williams, J.P.Allen. Individual Interactions Influence the Crystalline Order For Membrane Proteins. Acta Crystallogr.,Sect.D V. 57 1281 2001.
ISSN: ISSN 0907-4449
PubMed: 11526320
DOI: 10.1107/S090744490101109X