Magnesium in PDB 1jgz: Photosynthetic Reaction Center Mutant with Tyr M 76 Replaced with Lys
Protein crystallography data
The structure of Photosynthetic Reaction Center Mutant with Tyr M 76 Replaced with Lys, PDB code: 1jgz
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)
|
28.64 /
2.70
|
Space group
|
P 31 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
142.610,
142.610,
187.610,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
21.5 /
24.9
|
Other elements in 1jgz:
The structure of Photosynthetic Reaction Center Mutant with Tyr M 76 Replaced with Lys also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Photosynthetic Reaction Center Mutant with Tyr M 76 Replaced with Lys
(pdb code 1jgz). 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 Tyr M 76 Replaced with Lys, PDB code: 1jgz:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 1jgz
Go back to
Magnesium Binding Sites List in 1jgz
Magnesium binding site 1 out
of 4 in the Photosynthetic Reaction Center Mutant with Tyr M 76 Replaced with Lys
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 Tyr M 76 Replaced with Lys within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Mg850
b:38.8
occ:1.00
|
MG
|
L:BCL850
|
0.0
|
38.8
|
1.0
|
ND
|
L:BCL850
|
2.1
|
37.5
|
1.0
|
NA
|
L:BCL850
|
2.1
|
41.0
|
1.0
|
NC
|
L:BCL850
|
2.1
|
37.8
|
1.0
|
NB
|
L:BCL850
|
2.1
|
39.8
|
1.0
|
NE2
|
M:HIS182
|
2.7
|
43.1
|
1.0
|
C4A
|
L:BCL850
|
3.0
|
41.5
|
1.0
|
C1B
|
L:BCL850
|
3.1
|
40.9
|
1.0
|
C1C
|
L:BCL850
|
3.1
|
37.6
|
1.0
|
C1D
|
L:BCL850
|
3.1
|
37.2
|
1.0
|
C4D
|
L:BCL850
|
3.1
|
38.3
|
1.0
|
C4C
|
L:BCL850
|
3.1
|
37.2
|
1.0
|
C4B
|
L:BCL850
|
3.2
|
40.1
|
1.0
|
C1A
|
L:BCL850
|
3.2
|
42.3
|
1.0
|
CHB
|
L:BCL850
|
3.3
|
41.3
|
1.0
|
CHC
|
L:BCL850
|
3.4
|
39.3
|
1.0
|
CHD
|
L:BCL850
|
3.5
|
38.2
|
1.0
|
CHA
|
L:BCL850
|
3.5
|
40.8
|
1.0
|
CD2
|
M:HIS182
|
3.5
|
43.0
|
1.0
|
CE1
|
M:HIS182
|
3.7
|
43.2
|
1.0
|
C2D
|
L:BCL850
|
4.3
|
36.1
|
1.0
|
C2B
|
L:BCL850
|
4.3
|
41.9
|
1.0
|
C3A
|
L:BCL850
|
4.3
|
42.5
|
1.0
|
C3D
|
L:BCL850
|
4.4
|
36.0
|
1.0
|
C2C
|
L:BCL850
|
4.4
|
36.6
|
1.0
|
C3B
|
L:BCL850
|
4.4
|
43.2
|
1.0
|
C3C
|
L:BCL850
|
4.4
|
35.6
|
1.0
|
C2A
|
L:BCL850
|
4.4
|
44.4
|
1.0
|
OBB
|
M:BPH854
|
4.6
|
58.0
|
1.0
|
CG
|
M:HIS182
|
4.7
|
42.5
|
1.0
|
ND1
|
M:HIS182
|
4.8
|
43.4
|
1.0
|
CE2
|
L:PHE181
|
4.8
|
39.7
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 1jgz
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Magnesium Binding Sites List in 1jgz
Magnesium binding site 2 out
of 4 in the Photosynthetic Reaction Center Mutant with Tyr M 76 Replaced with Lys
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 Tyr M 76 Replaced with Lys within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Mg851
b:42.6
occ:1.00
|
MG
|
L:BCL851
|
0.0
|
42.6
|
1.0
|
ND
|
L:BCL851
|
2.0
|
43.6
|
1.0
|
NC
|
L:BCL851
|
2.1
|
42.4
|
1.0
|
NA
|
L:BCL851
|
2.1
|
43.6
|
1.0
|
NB
|
L:BCL851
|
2.1
|
42.2
|
1.0
|
NE2
|
L:HIS173
|
2.7
|
33.3
|
1.0
|
C4A
|
L:BCL851
|
3.0
|
42.9
|
1.0
|
C1B
|
L:BCL851
|
3.1
|
41.8
|
1.0
|
C4D
|
L:BCL851
|
3.1
|
44.8
|
1.0
|
C1D
|
L:BCL851
|
3.1
|
43.4
|
1.0
|
C1C
|
L:BCL851
|
3.1
|
41.1
|
1.0
|
C4C
|
L:BCL851
|
3.1
|
40.2
|
1.0
|
C4B
|
L:BCL851
|
3.2
|
40.4
|
1.0
|
C1A
|
L:BCL851
|
3.2
|
42.8
|
1.0
|
CHB
|
L:BCL851
|
3.3
|
43.0
|
1.0
|
CHC
|
L:BCL851
|
3.4
|
39.9
|
1.0
|
CAB
|
M:BCL852
|
3.4
|
43.0
|
1.0
|
CHD
|
L:BCL851
|
3.5
|
40.8
|
1.0
|
OBB
|
M:BCL852
|
3.5
|
41.7
|
1.0
|
CBB
|
M:BCL852
|
3.5
|
42.8
|
1.0
|
CHA
|
L:BCL851
|
3.5
|
44.1
|
1.0
|
CD2
|
L:HIS173
|
3.6
|
34.3
|
1.0
|
CE1
|
L:HIS173
|
3.7
|
33.7
|
1.0
|
C3B
|
M:BCL852
|
4.2
|
42.8
|
1.0
|
C2D
|
L:BCL851
|
4.3
|
44.2
|
1.0
|
C2B
|
L:BCL851
|
4.3
|
41.1
|
1.0
|
C3D
|
L:BCL851
|
4.3
|
45.4
|
1.0
|
C3A
|
L:BCL851
|
4.3
|
42.8
|
1.0
|
C3B
|
L:BCL851
|
4.4
|
40.3
|
1.0
|
C3C
|
L:BCL851
|
4.4
|
38.6
|
1.0
|
C2C
|
L:BCL851
|
4.4
|
39.2
|
1.0
|
C2A
|
L:BCL851
|
4.5
|
42.4
|
1.0
|
CG
|
L:HIS173
|
4.8
|
35.3
|
1.0
|
ND1
|
L:HIS173
|
4.8
|
35.0
|
1.0
|
C4B
|
M:BCL852
|
4.9
|
42.4
|
1.0
|
C2B
|
M:BCL852
|
4.9
|
42.7
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 1jgz
Go back to
Magnesium Binding Sites List in 1jgz
Magnesium binding site 3 out
of 4 in the Photosynthetic Reaction Center Mutant with Tyr M 76 Replaced with Lys
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 Tyr M 76 Replaced with Lys within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
M:Mg852
b:44.3
occ:1.00
|
MG
|
M:BCL852
|
0.0
|
44.3
|
1.0
|
ND
|
M:BCL852
|
2.0
|
43.8
|
1.0
|
NB
|
M:BCL852
|
2.1
|
43.6
|
1.0
|
NC
|
M:BCL852
|
2.1
|
45.3
|
1.0
|
NA
|
M:BCL852
|
2.1
|
43.5
|
1.0
|
NE2
|
M:HIS202
|
2.7
|
31.4
|
1.0
|
C4D
|
M:BCL852
|
3.0
|
43.9
|
1.0
|
C4A
|
M:BCL852
|
3.0
|
43.1
|
1.0
|
C1B
|
M:BCL852
|
3.0
|
43.3
|
1.0
|
C1C
|
M:BCL852
|
3.1
|
44.6
|
1.0
|
C1D
|
M:BCL852
|
3.1
|
44.5
|
1.0
|
C4B
|
M:BCL852
|
3.1
|
42.4
|
1.0
|
C4C
|
M:BCL852
|
3.1
|
44.9
|
1.0
|
C1A
|
M:BCL852
|
3.2
|
44.1
|
1.0
|
CHB
|
M:BCL852
|
3.3
|
43.0
|
1.0
|
CHC
|
M:BCL852
|
3.3
|
43.9
|
1.0
|
CHA
|
M:BCL852
|
3.5
|
44.3
|
1.0
|
CHD
|
M:BCL852
|
3.5
|
44.6
|
1.0
|
CE1
|
M:HIS202
|
3.5
|
32.4
|
1.0
|
CAB
|
L:BCL851
|
3.6
|
38.8
|
1.0
|
OBB
|
L:BCL851
|
3.7
|
39.4
|
1.0
|
CBB
|
L:BCL851
|
3.8
|
38.0
|
1.0
|
CD2
|
M:HIS202
|
3.8
|
33.7
|
1.0
|
C2D
|
M:BCL852
|
4.3
|
44.6
|
1.0
|
C2B
|
M:BCL852
|
4.3
|
42.7
|
1.0
|
C3B
|
L:BCL851
|
4.3
|
40.3
|
1.0
|
C3D
|
M:BCL852
|
4.3
|
44.4
|
1.0
|
C3A
|
M:BCL852
|
4.4
|
43.7
|
1.0
|
C3B
|
M:BCL852
|
4.4
|
42.8
|
1.0
|
C2C
|
M:BCL852
|
4.4
|
43.1
|
1.0
|
C3C
|
M:BCL852
|
4.4
|
43.3
|
1.0
|
C2A
|
M:BCL852
|
4.5
|
44.5
|
1.0
|
ND1
|
M:HIS202
|
4.7
|
33.9
|
1.0
|
CG
|
M:HIS202
|
4.9
|
35.0
|
1.0
|
CBD
|
M:BCL852
|
4.9
|
44.0
|
1.0
|
C4B
|
L:BCL851
|
5.0
|
40.4
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 1jgz
Go back to
Magnesium Binding Sites List in 1jgz
Magnesium binding site 4 out
of 4 in the Photosynthetic Reaction Center Mutant with Tyr M 76 Replaced with Lys
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 Tyr M 76 Replaced with Lys within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
M:Mg853
b:35.1
occ:1.00
|
MG
|
M:BCL853
|
0.0
|
35.1
|
1.0
|
ND
|
M:BCL853
|
2.0
|
32.3
|
1.0
|
NC
|
M:BCL853
|
2.0
|
33.7
|
1.0
|
NA
|
M:BCL853
|
2.1
|
33.4
|
1.0
|
NB
|
M:BCL853
|
2.1
|
34.1
|
1.0
|
NE2
|
L:HIS153
|
2.9
|
46.2
|
1.0
|
C4A
|
M:BCL853
|
3.0
|
33.9
|
1.0
|
C1C
|
M:BCL853
|
3.0
|
35.8
|
1.0
|
C1D
|
M:BCL853
|
3.1
|
33.3
|
1.0
|
C4D
|
M:BCL853
|
3.1
|
33.4
|
1.0
|
C1B
|
M:BCL853
|
3.1
|
33.7
|
1.0
|
C4C
|
M:BCL853
|
3.1
|
34.5
|
1.0
|
C4B
|
M:BCL853
|
3.1
|
35.9
|
1.0
|
C1A
|
M:BCL853
|
3.2
|
34.1
|
1.0
|
CHB
|
M:BCL853
|
3.3
|
32.2
|
1.0
|
CHC
|
M:BCL853
|
3.3
|
35.6
|
1.0
|
CHD
|
M:BCL853
|
3.4
|
33.3
|
1.0
|
CHA
|
M:BCL853
|
3.5
|
34.5
|
1.0
|
CD2
|
L:HIS153
|
3.8
|
47.9
|
1.0
|
CE1
|
L:HIS153
|
3.8
|
46.5
|
1.0
|
C2D
|
M:BCL853
|
4.3
|
34.6
|
1.0
|
C2B
|
M:BCL853
|
4.3
|
36.0
|
1.0
|
C3A
|
M:BCL853
|
4.3
|
35.2
|
1.0
|
C3D
|
M:BCL853
|
4.3
|
34.6
|
1.0
|
C3C
|
M:BCL853
|
4.4
|
35.8
|
1.0
|
C2C
|
M:BCL853
|
4.4
|
35.6
|
1.0
|
C3B
|
M:BCL853
|
4.4
|
37.7
|
1.0
|
C2A
|
M:BCL853
|
4.4
|
35.0
|
1.0
|
OBB
|
L:BPH855
|
4.5
|
48.6
|
1.0
|
CE2
|
M:TYR210
|
4.6
|
38.1
|
1.0
|
CAA
|
M:BCL853
|
4.9
|
39.5
|
1.0
|
ND1
|
L:HIS153
|
5.0
|
48.1
|
1.0
|
CBD
|
M:BCL853
|
5.0
|
36.5
|
1.0
|
|
Reference:
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
Page generated: Tue Aug 13 06:35:24 2024
|