Magnesium in PDB 1jgw: Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Leu

The structure of Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Leu, PDB code: 1jgw 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)	29.23 / 2.80
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	142.600, 142.600, 187.400, 90.00, 90.00, 120.00
R / Rfree (%)	21.1 / 23.7

The structure of Photosynthetic Reaction Center Mutant with Thr M 21 Replaced with Leu 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 Leu (pdb code 1jgw). 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 Leu, PDB code: 1jgw:
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 Leu


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 Leu within 5.0Å range: probe atom residue distance (Å) B Occ L:Mg850 b:31.8 occ:1.00 MG L:BCL850 0.0 31.8 1.0 ND L:BCL850 2.0 30.4 1.0 NC L:BCL850 2.1 31.9 1.0 NA L:BCL850 2.1 33.2 1.0 NB L:BCL850 2.1 33.3 1.0 NE2 M:HIS182 2.7 32.8 1.0 C4A L:BCL850 3.0 35.1 1.0 C4D L:BCL850 3.0 32.7 1.0 C1B L:BCL850 3.1 34.1 1.0 C1C L:BCL850 3.1 31.4 1.0 C1D L:BCL850 3.1 30.3 1.0 C4C L:BCL850 3.1 30.1 1.0 C4B L:BCL850 3.1 34.0 1.0 C1A L:BCL850 3.2 36.2 1.0 CHB L:BCL850 3.3 34.3 1.0 CHC L:BCL850 3.4 32.3 1.0 CD2 M:HIS182 3.4 34.1 1.0 CHD L:BCL850 3.5 30.5 1.0 CHA L:BCL850 3.5 34.4 1.0 CE1 M:HIS182 3.9 32.4 1.0 C2D L:BCL850 4.3 31.6 1.0 C2B L:BCL850 4.3 35.0 1.0 C3D L:BCL850 4.3 32.3 1.0 C3A L:BCL850 4.3 37.4 1.0 C3B L:BCL850 4.4 36.1 1.0 C2C L:BCL850 4.4 29.1 1.0 C3C L:BCL850 4.4 27.4 1.0 C2A L:BCL850 4.4 39.7 1.0 OBB M:BPH854 4.6 46.0 1.0 CE2 L:PHE181 4.7 27.8 1.0 CG M:HIS182 4.7 33.4 1.0 ND1 M:HIS182 4.9 33.0 1.0 CBD L:BCL850 5.0 34.9 1.0

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


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 Leu within 5.0Å range: probe atom residue distance (Å) B Occ L:Mg851 b:33.8 occ:1.00 MG L:BCL851 0.0 33.8 1.0 ND L:BCL851 2.0 34.4 1.0 NC L:BCL851 2.1 32.6 1.0 NB L:BCL851 2.1 31.9 1.0 NA L:BCL851 2.1 33.8 1.0 NE2 L:HIS173 2.6 26.1 1.0 C4A L:BCL851 3.0 32.6 1.0 C4D L:BCL851 3.1 35.0 1.0 C1B L:BCL851 3.1 32.0 1.0 C1D L:BCL851 3.1 34.0 1.0 C1C L:BCL851 3.1 32.3 1.0 C4C L:BCL851 3.1 31.6 1.0 C4B L:BCL851 3.1 31.4 1.0 C1A L:BCL851 3.2 33.4 1.0 CHB L:BCL851 3.3 31.4 1.0 CHC L:BCL851 3.4 31.9 1.0 OBB M:BCL852 3.4 38.9 1.0 CAB M:BCL852 3.4 34.8 1.0 CE1 L:HIS173 3.4 25.9 1.0 CHD L:BCL851 3.5 32.4 1.0 CHA L:BCL851 3.5 35.4 1.0 CBB M:BCL852 3.5 35.8 1.0 CD2 L:HIS173 3.7 26.8 1.0 C3B M:BCL852 4.2 32.9 1.0 C2D L:BCL851 4.3 34.0 1.0 C2B L:BCL851 4.3 32.9 1.0 C3D L:BCL851 4.3 35.0 1.0 C3A L:BCL851 4.4 33.9 1.0 C3B L:BCL851 4.4 32.4 1.0 C2C L:BCL851 4.4 29.0 1.0 C3C L:BCL851 4.4 30.4 1.0 C2A L:BCL851 4.5 33.4 1.0 ND1 L:HIS173 4.6 25.8 1.0 CG L:HIS173 4.8 27.3 1.0 C4B M:BCL852 5.0 31.3 1.0

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


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 Leu within 5.0Å range: probe atom residue distance (Å) B Occ M:Mg852 b:32.4 occ:1.00 MG M:BCL852 0.0 32.4 1.0 ND M:BCL852 2.0 31.7 1.0 NC M:BCL852 2.1 32.0 1.0 NB M:BCL852 2.1 31.5 1.0 NA M:BCL852 2.1 31.0 1.0 NE2 M:HIS202 2.7 25.9 1.0 C4D M:BCL852 3.0 32.5 1.0 C4A M:BCL852 3.1 30.3 1.0 C1B M:BCL852 3.1 31.8 1.0 C1C M:BCL852 3.1 32.1 1.0 C1D M:BCL852 3.1 31.9 1.0 C4B M:BCL852 3.1 31.3 1.0 C4C M:BCL852 3.1 31.3 1.0 C1A M:BCL852 3.2 30.9 1.0 CHC M:BCL852 3.3 31.7 1.0 CHB M:BCL852 3.3 30.4 1.0 CE1 M:HIS202 3.5 23.9 1.0 CHA M:BCL852 3.5 31.6 1.0 CHD M:BCL852 3.5 31.1 1.0 CAB L:BCL851 3.6 33.0 1.0 CBB L:BCL851 3.7 34.9 1.0 OBB L:BCL851 3.8 35.3 1.0 CD2 M:HIS202 3.8 26.5 1.0 C2D M:BCL852 4.3 31.7 1.0 C2B M:BCL852 4.3 32.2 1.0 C3D M:BCL852 4.3 32.1 1.0 C3B L:BCL851 4.3 32.4 1.0 C3B M:BCL852 4.4 32.9 1.0 C3A M:BCL852 4.4 30.9 1.0 C2C M:BCL852 4.4 32.2 1.0 C3C M:BCL852 4.4 31.0 1.0 C2A M:BCL852 4.5 31.3 1.0 ND1 M:HIS202 4.7 23.7 1.0 CG M:HIS202 4.9 25.4 1.0 CBD M:BCL852 5.0 30.7 1.0

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


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 Leu within 5.0Å range: probe atom residue distance (Å) B Occ M:Mg853 b:23.1 occ:1.00 MG M:BCL853 0.0 23.1 1.0 ND M:BCL853 2.0 22.0 1.0 NA M:BCL853 2.0 23.7 1.0 NC M:BCL853 2.0 21.2 1.0 NB M:BCL853 2.1 22.7 1.0 NE2 L:HIS153 2.9 40.5 1.0 C4A M:BCL853 3.0 24.4 1.0 C1C M:BCL853 3.0 24.6 1.0 C4D M:BCL853 3.1 23.4 1.0 C1B M:BCL853 3.1 23.5 1.0 C1D M:BCL853 3.1 23.4 1.0 C4C M:BCL853 3.1 23.1 1.0 C4B M:BCL853 3.1 23.6 1.0 C1A M:BCL853 3.1 26.2 1.0 CHB M:BCL853 3.3 22.5 1.0 CHC M:BCL853 3.3 22.9 1.0 CHD M:BCL853 3.4 23.2 1.0 CHA M:BCL853 3.5 25.7 1.0 CD2 L:HIS153 3.6 41.5 1.0 CE1 L:HIS153 4.0 41.2 1.0 C2D M:BCL853 4.3 22.4 1.0 OBB L:BPH855 4.3 37.3 1.0 C3A M:BCL853 4.3 27.1 1.0 C2B M:BCL853 4.3 23.8 1.0 C3D M:BCL853 4.3 24.2 1.0 C3C M:BCL853 4.4 25.2 1.0 C2C M:BCL853 4.4 25.6 1.0 C2A M:BCL853 4.4 27.7 1.0 C3B M:BCL853 4.4 25.0 1.0 CE2 M:TYR210 4.7 31.0 1.0 CAA M:BCL853 4.9 30.2 1.0 CG L:HIS153 4.9 41.9 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