Magnesium in PDB 5hpz: Type II Water Soluble Chl Binding Proteins
Protein crystallography data
The structure of Type II Water Soluble Chl Binding Proteins, PDB code: 5hpz
was solved by
D.Bednarczyk,
O.Dym,
V.Prabahard,
D.Noy,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
68.59 /
1.96
|
Space group
|
P 2 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
38.920,
95.479,
98.610,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21 /
26.6
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Type II Water Soluble Chl Binding Proteins
(pdb code 5hpz). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the
Type II Water Soluble Chl Binding Proteins, PDB code: 5hpz:
Jump to Magnesium binding site number:
1;
2;
Magnesium binding site 1 out
of 2 in 5hpz
Go back to
Magnesium Binding Sites List in 5hpz
Magnesium binding site 1 out
of 2 in the Type II Water Soluble Chl Binding Proteins
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Type II Water Soluble Chl Binding Proteins within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1001
b:35.0
occ:1.00
|
MG
|
A:68G1001
|
0.0
|
35.0
|
1.0
|
NB
|
A:68G1001
|
2.0
|
27.1
|
1.0
|
ND
|
A:68G1001
|
2.0
|
31.7
|
1.0
|
NC
|
A:68G1001
|
2.0
|
34.6
|
1.0
|
NA
|
A:68G1001
|
2.2
|
23.9
|
1.0
|
O
|
A:PRO32
|
2.5
|
26.2
|
1.0
|
C1B
|
A:68G1001
|
2.9
|
27.6
|
1.0
|
C4B
|
A:68G1001
|
3.0
|
28.7
|
1.0
|
C1D
|
A:68G1001
|
3.0
|
29.7
|
1.0
|
C4D
|
A:68G1001
|
3.0
|
29.6
|
1.0
|
C1C
|
A:68G1001
|
3.0
|
27.8
|
1.0
|
C4A
|
A:68G1001
|
3.0
|
24.1
|
1.0
|
C4C
|
A:68G1001
|
3.0
|
28.8
|
1.0
|
CHB
|
A:68G1001
|
3.2
|
23.3
|
1.0
|
C1A
|
A:68G1001
|
3.3
|
26.7
|
1.0
|
CHC
|
A:68G1001
|
3.3
|
29.9
|
1.0
|
CHD
|
A:68G1001
|
3.3
|
30.7
|
1.0
|
CHA
|
A:68G1001
|
3.5
|
28.8
|
1.0
|
C
|
A:PRO32
|
3.6
|
24.4
|
1.0
|
C9
|
B:68G1001
|
3.8
|
53.2
|
1.0
|
C2B
|
A:68G1001
|
4.1
|
29.1
|
1.0
|
C3B
|
A:68G1001
|
4.1
|
28.1
|
1.0
|
C2D
|
A:68G1001
|
4.1
|
31.2
|
1.0
|
CA
|
A:ALA33
|
4.1
|
25.9
|
1.0
|
C2C
|
A:68G1001
|
4.2
|
33.1
|
1.0
|
C3D
|
A:68G1001
|
4.2
|
32.3
|
1.0
|
C3C
|
A:68G1001
|
4.2
|
30.0
|
1.0
|
C6
|
B:68G1001
|
4.3
|
51.4
|
1.0
|
N
|
A:ALA33
|
4.3
|
23.4
|
1.0
|
C3A
|
A:68G1001
|
4.3
|
26.1
|
1.0
|
C2A
|
A:68G1001
|
4.5
|
27.1
|
1.0
|
CB
|
A:ALA33
|
4.5
|
26.5
|
1.0
|
CA
|
A:PRO32
|
4.6
|
25.5
|
1.0
|
CB
|
A:PRO32
|
4.7
|
26.6
|
1.0
|
C8
|
B:68G1001
|
4.7
|
53.0
|
1.0
|
CED
|
B:68G1001
|
4.7
|
31.3
|
1.0
|
CG2
|
A:VAL31
|
4.8
|
28.8
|
1.0
|
N
|
A:PRO32
|
4.9
|
24.9
|
1.0
|
CBD
|
A:68G1001
|
4.9
|
31.3
|
1.0
|
CD
|
A:PRO32
|
5.0
|
25.6
|
1.0
|
|
Magnesium binding site 2 out
of 2 in 5hpz
Go back to
Magnesium Binding Sites List in 5hpz
Magnesium binding site 2 out
of 2 in the Type II Water Soluble Chl Binding Proteins
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Type II Water Soluble Chl Binding Proteins within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1001
b:33.3
occ:1.00
|
MG
|
B:68G1001
|
0.0
|
33.3
|
1.0
|
NB
|
B:68G1001
|
2.0
|
25.7
|
1.0
|
ND
|
B:68G1001
|
2.0
|
26.1
|
1.0
|
NC
|
B:68G1001
|
2.2
|
25.4
|
1.0
|
NA
|
B:68G1001
|
2.2
|
22.6
|
1.0
|
O
|
B:PRO32
|
2.5
|
23.6
|
1.0
|
C1B
|
B:68G1001
|
2.9
|
25.9
|
1.0
|
C4B
|
B:68G1001
|
3.0
|
25.1
|
1.0
|
C4D
|
B:68G1001
|
3.0
|
24.7
|
1.0
|
C1D
|
B:68G1001
|
3.0
|
27.8
|
1.0
|
C4A
|
B:68G1001
|
3.0
|
23.5
|
1.0
|
C1C
|
B:68G1001
|
3.1
|
21.8
|
1.0
|
C4C
|
B:68G1001
|
3.1
|
26.1
|
1.0
|
CHB
|
B:68G1001
|
3.2
|
24.7
|
1.0
|
C1A
|
B:68G1001
|
3.2
|
24.1
|
1.0
|
CHC
|
B:68G1001
|
3.3
|
24.2
|
1.0
|
CHD
|
B:68G1001
|
3.4
|
26.3
|
1.0
|
CHA
|
B:68G1001
|
3.5
|
24.7
|
1.0
|
C
|
B:PRO32
|
3.6
|
22.6
|
1.0
|
C9
|
A:68G1001
|
4.0
|
46.5
|
1.0
|
C2B
|
B:68G1001
|
4.1
|
26.0
|
1.0
|
C3B
|
B:68G1001
|
4.1
|
26.1
|
1.0
|
CA
|
B:ALA33
|
4.1
|
26.4
|
1.0
|
C2D
|
B:68G1001
|
4.1
|
26.9
|
1.0
|
C3D
|
B:68G1001
|
4.2
|
27.1
|
1.0
|
C2C
|
B:68G1001
|
4.2
|
27.3
|
1.0
|
C3C
|
B:68G1001
|
4.3
|
26.7
|
1.0
|
N
|
B:ALA33
|
4.3
|
23.9
|
1.0
|
C3A
|
B:68G1001
|
4.3
|
23.7
|
1.0
|
C2A
|
B:68G1001
|
4.4
|
25.1
|
1.0
|
C6
|
A:68G1001
|
4.4
|
48.5
|
1.0
|
CB
|
B:ALA33
|
4.6
|
25.1
|
1.0
|
CED
|
A:68G1001
|
4.6
|
34.2
|
1.0
|
CA
|
B:PRO32
|
4.7
|
23.3
|
1.0
|
CB
|
B:PRO32
|
4.7
|
24.5
|
1.0
|
N
|
B:PRO32
|
4.8
|
25.0
|
1.0
|
CG2
|
B:VAL31
|
4.8
|
26.0
|
1.0
|
C8
|
A:68G1001
|
4.9
|
47.5
|
1.0
|
CBD
|
B:68G1001
|
4.9
|
28.2
|
1.0
|
CD
|
B:PRO32
|
5.0
|
23.9
|
1.0
|
|
Reference:
D.Bednarczyk,
O.Dym,
V.Prabahar,
Y.Peleg,
D.H.Pike,
D.Noy.
Fine Tuning of Chlorophyll Spectra By Protein-Induced Ring Deformation. Angew.Chem.Int.Ed.Engl. V. 55 6901 2016.
ISSN: ESSN 1521-3773
PubMed: 27098554
DOI: 10.1002/ANIE.201512001
Page generated: Sun Sep 29 16:04:55 2024
|