Magnesium in PDB 1jh0: Photosynthetic Reaction Center Mutant with Glu L 205 Replaced to Leu
Protein crystallography data
The structure of Photosynthetic Reaction Center Mutant with Glu L 205 Replaced to Leu, PDB code: 1jh0
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)
|
29.90 /
3.50
|
Space group
|
P 31 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
141.800,
141.800,
187.400,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
22.5 /
26.9
|
Other elements in 1jh0:
The structure of Photosynthetic Reaction Center Mutant with Glu L 205 Replaced to Leu also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Photosynthetic Reaction Center Mutant with Glu L 205 Replaced to Leu
(pdb code 1jh0). 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 Glu L 205 Replaced to Leu, PDB code: 1jh0:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 1jh0
Go back to
Magnesium Binding Sites List in 1jh0
Magnesium binding site 1 out
of 4 in the Photosynthetic Reaction Center Mutant with Glu L 205 Replaced to 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 Glu L 205 Replaced to Leu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Mg851
b:54.7
occ:1.00
|
MG
|
L:BCL851
|
0.0
|
54.7
|
1.0
|
ND
|
L:BCL851
|
2.0
|
53.9
|
1.0
|
NC
|
L:BCL851
|
2.1
|
63.6
|
1.0
|
NA
|
L:BCL851
|
2.1
|
56.7
|
1.0
|
NB
|
L:BCL851
|
2.1
|
54.8
|
1.0
|
NE2
|
L:HIS173
|
2.6
|
35.3
|
1.0
|
C4A
|
L:BCL851
|
3.0
|
55.5
|
1.0
|
C4D
|
L:BCL851
|
3.1
|
61.2
|
1.0
|
C1B
|
L:BCL851
|
3.1
|
52.1
|
1.0
|
C1D
|
L:BCL851
|
3.1
|
47.3
|
1.0
|
C1C
|
L:BCL851
|
3.1
|
67.0
|
1.0
|
C4C
|
L:BCL851
|
3.1
|
57.4
|
1.0
|
C4B
|
L:BCL851
|
3.1
|
51.5
|
1.0
|
C1A
|
L:BCL851
|
3.2
|
55.2
|
1.0
|
CHB
|
L:BCL851
|
3.3
|
48.3
|
1.0
|
CHC
|
L:BCL851
|
3.4
|
57.7
|
1.0
|
CHD
|
L:BCL851
|
3.5
|
53.9
|
1.0
|
CHA
|
L:BCL851
|
3.5
|
64.4
|
1.0
|
CAB
|
M:BCL852
|
3.5
|
75.6
|
1.0
|
CD2
|
L:HIS173
|
3.6
|
50.6
|
1.0
|
OBB
|
M:BCL852
|
3.6
|
79.6
|
1.0
|
CE1
|
L:HIS173
|
3.6
|
49.5
|
1.0
|
CBB
|
M:BCL852
|
3.6
|
76.9
|
1.0
|
C3B
|
M:BCL852
|
4.2
|
68.2
|
1.0
|
C2D
|
L:BCL851
|
4.3
|
41.0
|
1.0
|
C2B
|
L:BCL851
|
4.3
|
56.2
|
1.0
|
C3D
|
L:BCL851
|
4.3
|
53.4
|
1.0
|
C3A
|
L:BCL851
|
4.3
|
59.2
|
1.0
|
C3B
|
L:BCL851
|
4.4
|
50.9
|
1.0
|
C3C
|
L:BCL851
|
4.4
|
63.1
|
1.0
|
C2C
|
L:BCL851
|
4.4
|
60.1
|
1.0
|
C2A
|
L:BCL851
|
4.5
|
52.5
|
1.0
|
ND1
|
L:HIS173
|
4.7
|
54.0
|
1.0
|
CG
|
L:HIS173
|
4.7
|
55.3
|
1.0
|
CD2
|
L:PHE167
|
4.9
|
61.7
|
1.0
|
C4B
|
M:BCL852
|
5.0
|
64.2
|
1.0
|
CBD
|
L:BCL851
|
5.0
|
66.1
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 1jh0
Go back to
Magnesium Binding Sites List in 1jh0
Magnesium binding site 2 out
of 4 in the Photosynthetic Reaction Center Mutant with Glu L 205 Replaced to 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 Glu L 205 Replaced to Leu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Mg853
b:30.9
occ:1.00
|
MG
|
L:BCL853
|
0.0
|
30.9
|
1.0
|
ND
|
L:BCL853
|
2.0
|
30.4
|
1.0
|
NA
|
L:BCL853
|
2.0
|
36.1
|
1.0
|
NC
|
L:BCL853
|
2.0
|
33.4
|
1.0
|
NB
|
L:BCL853
|
2.1
|
33.7
|
1.0
|
NE2
|
L:HIS153
|
2.8
|
68.7
|
1.0
|
C4A
|
L:BCL853
|
3.0
|
40.2
|
1.0
|
C1B
|
L:BCL853
|
3.1
|
25.7
|
1.0
|
C1D
|
L:BCL853
|
3.1
|
35.2
|
1.0
|
C1C
|
L:BCL853
|
3.1
|
36.8
|
1.0
|
C4D
|
L:BCL853
|
3.1
|
31.4
|
1.0
|
C4C
|
L:BCL853
|
3.1
|
31.3
|
1.0
|
C4B
|
L:BCL853
|
3.2
|
30.6
|
1.0
|
C1A
|
L:BCL853
|
3.2
|
41.7
|
1.0
|
CHB
|
L:BCL853
|
3.3
|
29.5
|
1.0
|
CHC
|
L:BCL853
|
3.4
|
35.3
|
1.0
|
CHD
|
L:BCL853
|
3.4
|
30.7
|
1.0
|
CHA
|
L:BCL853
|
3.5
|
33.0
|
1.0
|
CD2
|
L:HIS153
|
3.6
|
76.7
|
1.0
|
CE1
|
L:HIS153
|
3.9
|
71.7
|
1.0
|
C2D
|
L:BCL853
|
4.3
|
32.3
|
1.0
|
C3A
|
L:BCL853
|
4.3
|
52.7
|
1.0
|
C2B
|
L:BCL853
|
4.3
|
22.1
|
1.0
|
C3D
|
L:BCL853
|
4.3
|
31.7
|
1.0
|
C3C
|
L:BCL853
|
4.4
|
43.4
|
1.0
|
C2C
|
L:BCL853
|
4.4
|
40.7
|
1.0
|
OBB
|
L:BPH855
|
4.4
|
79.6
|
1.0
|
C2A
|
L:BCL853
|
4.4
|
45.8
|
1.0
|
C3B
|
L:BCL853
|
4.4
|
26.1
|
1.0
|
CE2
|
M:TYR210
|
4.9
|
54.8
|
1.0
|
CG
|
L:HIS153
|
4.9
|
79.1
|
1.0
|
CAA
|
L:BCL853
|
4.9
|
54.2
|
1.0
|
ND1
|
L:HIS153
|
5.0
|
78.1
|
1.0
|
CBC
|
L:BCL853
|
5.0
|
49.7
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 1jh0
Go back to
Magnesium Binding Sites List in 1jh0
Magnesium binding site 3 out
of 4 in the Photosynthetic Reaction Center Mutant with Glu L 205 Replaced to 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 Glu L 205 Replaced to Leu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
M:Mg850
b:46.1
occ:1.00
|
MG
|
M:BCL850
|
0.0
|
46.1
|
1.0
|
ND
|
M:BCL850
|
2.0
|
49.9
|
1.0
|
NC
|
M:BCL850
|
2.0
|
43.9
|
1.0
|
NA
|
M:BCL850
|
2.0
|
53.1
|
1.0
|
NB
|
M:BCL850
|
2.1
|
58.5
|
1.0
|
NE2
|
M:HIS182
|
2.5
|
51.3
|
1.0
|
C1B
|
M:BCL850
|
3.0
|
57.9
|
1.0
|
C4A
|
M:BCL850
|
3.0
|
53.9
|
1.0
|
C1C
|
M:BCL850
|
3.0
|
41.4
|
1.0
|
C4D
|
M:BCL850
|
3.1
|
52.5
|
1.0
|
C1D
|
M:BCL850
|
3.1
|
54.9
|
1.0
|
C4C
|
M:BCL850
|
3.1
|
46.5
|
1.0
|
C4B
|
M:BCL850
|
3.2
|
54.9
|
1.0
|
C1A
|
M:BCL850
|
3.2
|
61.8
|
1.0
|
CHB
|
M:BCL850
|
3.2
|
48.3
|
1.0
|
CHC
|
M:BCL850
|
3.3
|
45.8
|
1.0
|
CD2
|
M:HIS182
|
3.4
|
54.6
|
1.0
|
CHD
|
M:BCL850
|
3.4
|
51.7
|
1.0
|
CHA
|
M:BCL850
|
3.5
|
58.4
|
1.0
|
CE1
|
M:HIS182
|
3.6
|
58.2
|
1.0
|
C2B
|
M:BCL850
|
4.2
|
60.9
|
1.0
|
C2D
|
M:BCL850
|
4.3
|
51.7
|
1.0
|
C3A
|
M:BCL850
|
4.3
|
66.2
|
1.0
|
C3D
|
M:BCL850
|
4.3
|
53.3
|
1.0
|
C2C
|
M:BCL850
|
4.4
|
38.5
|
1.0
|
C3C
|
M:BCL850
|
4.4
|
40.1
|
1.0
|
C2A
|
M:BCL850
|
4.4
|
69.4
|
1.0
|
CG
|
M:HIS182
|
4.6
|
62.9
|
1.0
|
C3B
|
M:BCL850
|
4.6
|
66.0
|
1.0
|
ND1
|
M:HIS182
|
4.6
|
63.3
|
1.0
|
OBB
|
M:BPH854
|
4.7
|
79.6
|
1.0
|
CE2
|
L:PHE181
|
4.8
|
59.2
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 1jh0
Go back to
Magnesium Binding Sites List in 1jh0
Magnesium binding site 4 out
of 4 in the Photosynthetic Reaction Center Mutant with Glu L 205 Replaced to 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 Glu L 205 Replaced to Leu within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
M:Mg852
b:52.2
occ:1.00
|
MG
|
M:BCL852
|
0.0
|
52.2
|
1.0
|
ND
|
M:BCL852
|
2.0
|
60.4
|
1.0
|
NB
|
M:BCL852
|
2.1
|
63.2
|
1.0
|
NC
|
M:BCL852
|
2.1
|
66.0
|
1.0
|
NA
|
M:BCL852
|
2.1
|
52.9
|
1.0
|
NE2
|
M:HIS202
|
2.6
|
45.2
|
1.0
|
C4A
|
M:BCL852
|
3.0
|
57.3
|
1.0
|
C1B
|
M:BCL852
|
3.0
|
69.1
|
1.0
|
C4D
|
M:BCL852
|
3.0
|
58.4
|
1.0
|
C1C
|
M:BCL852
|
3.1
|
68.6
|
1.0
|
C1D
|
M:BCL852
|
3.1
|
56.5
|
1.0
|
C4B
|
M:BCL852
|
3.1
|
64.2
|
1.0
|
C4C
|
M:BCL852
|
3.1
|
57.5
|
1.0
|
C1A
|
M:BCL852
|
3.2
|
48.2
|
1.0
|
CHB
|
M:BCL852
|
3.3
|
66.0
|
1.0
|
CHC
|
M:BCL852
|
3.3
|
68.1
|
1.0
|
CE1
|
M:HIS202
|
3.4
|
51.0
|
1.0
|
CHD
|
M:BCL852
|
3.5
|
50.3
|
1.0
|
CHA
|
M:BCL852
|
3.5
|
51.1
|
1.0
|
CD2
|
M:HIS202
|
3.6
|
45.9
|
1.0
|
CAB
|
L:BCL851
|
3.7
|
51.6
|
1.0
|
CBB
|
L:BCL851
|
3.8
|
57.2
|
1.0
|
OBB
|
L:BCL851
|
3.9
|
56.3
|
1.0
|
C2D
|
M:BCL852
|
4.2
|
61.4
|
1.0
|
C2B
|
M:BCL852
|
4.3
|
70.5
|
1.0
|
C3D
|
M:BCL852
|
4.3
|
59.0
|
1.0
|
C3A
|
M:BCL852
|
4.4
|
55.6
|
1.0
|
C3B
|
M:BCL852
|
4.4
|
68.2
|
1.0
|
C3B
|
L:BCL851
|
4.4
|
50.9
|
1.0
|
C2C
|
M:BCL852
|
4.4
|
64.0
|
1.0
|
C3C
|
M:BCL852
|
4.4
|
60.7
|
1.0
|
C2A
|
M:BCL852
|
4.5
|
48.7
|
1.0
|
ND1
|
M:HIS202
|
4.5
|
47.8
|
1.0
|
CG
|
M:HIS202
|
4.7
|
45.5
|
1.0
|
CD1
|
M:ILE206
|
4.7
|
66.4
|
1.0
|
CBD
|
M:BCL852
|
5.0
|
52.0
|
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 06:35:25 2024
|