Magnesium in PDB 2wjh: Structure and Function of the Feob G-Domain From Methanococcus Jannaschii
Protein crystallography data
The structure of Structure and Function of the Feob G-Domain From Methanococcus Jannaschii, PDB code: 2wjh
was solved by
S.Koester,
M.Wehner,
C.Herrmann,
W.Kuehlbrandt,
O.Yildiz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
42.944 /
2.10
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
104.200,
50.400,
94.700,
90.00,
120.60,
90.00
|
R / Rfree (%)
|
21.04 /
24.61
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure and Function of the Feob G-Domain From Methanococcus Jannaschii
(pdb code 2wjh). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the
Structure and Function of the Feob G-Domain From Methanococcus Jannaschii, PDB code: 2wjh:
Jump to Magnesium binding site number:
1;
2;
3;
Magnesium binding site 1 out
of 3 in 2wjh
Go back to
Magnesium Binding Sites List in 2wjh
Magnesium binding site 1 out
of 3 in the Structure and Function of the Feob G-Domain From Methanococcus Jannaschii
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Structure and Function of the Feob G-Domain From Methanococcus Jannaschii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1167
b:40.6
occ:1.00
|
O
|
A:HOH2016
|
2.4
|
42.8
|
1.0
|
O
|
A:HOH2011
|
2.5
|
44.7
|
1.0
|
O
|
A:GLY25
|
2.6
|
49.0
|
1.0
|
O
|
A:THR24
|
2.7
|
32.5
|
1.0
|
OG1
|
A:THR24
|
2.7
|
31.6
|
1.0
|
O
|
A:ASN21
|
2.7
|
24.7
|
1.0
|
C
|
A:THR24
|
3.2
|
32.1
|
1.0
|
C
|
A:GLY25
|
3.4
|
47.8
|
1.0
|
MG
|
A:MG1168
|
3.6
|
57.3
|
1.0
|
CB
|
A:THR24
|
3.6
|
30.2
|
1.0
|
C
|
A:ASN21
|
3.7
|
25.2
|
1.0
|
CA
|
A:THR24
|
3.8
|
27.4
|
1.0
|
N
|
A:GLY25
|
3.9
|
35.9
|
1.0
|
CA
|
A:ASN21
|
4.0
|
24.6
|
1.0
|
CG2
|
A:VAL28
|
4.1
|
31.6
|
1.0
|
CA
|
A:GLY25
|
4.2
|
43.4
|
1.0
|
OE2
|
A:GLU26
|
4.2
|
68.1
|
1.0
|
N
|
A:THR24
|
4.2
|
27.9
|
1.0
|
N
|
A:GLU26
|
4.3
|
48.0
|
1.0
|
CA
|
A:GLU26
|
4.4
|
49.8
|
1.0
|
O
|
A:PHE20
|
4.5
|
16.4
|
1.0
|
CB
|
A:ASN21
|
4.6
|
26.3
|
1.0
|
OE1
|
A:GLU26
|
4.6
|
71.2
|
1.0
|
CD
|
A:GLU26
|
4.7
|
68.5
|
1.0
|
OD1
|
A:ASN21
|
4.8
|
37.5
|
1.0
|
N
|
A:ALA22
|
4.9
|
25.8
|
1.0
|
C
|
A:GLU26
|
5.0
|
45.5
|
1.0
|
CG2
|
A:THR24
|
5.0
|
28.6
|
1.0
|
|
Magnesium binding site 2 out
of 3 in 2wjh
Go back to
Magnesium Binding Sites List in 2wjh
Magnesium binding site 2 out
of 3 in the Structure and Function of the Feob G-Domain From Methanococcus Jannaschii
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Structure and Function of the Feob G-Domain From Methanococcus Jannaschii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1168
b:57.3
occ:1.00
|
O
|
A:HOH2014
|
2.5
|
52.5
|
1.0
|
O
|
A:HOH2016
|
2.5
|
42.8
|
1.0
|
O
|
A:HOH2002
|
2.5
|
40.7
|
1.0
|
O
|
A:THR24
|
2.6
|
32.5
|
1.0
|
O
|
A:ASN21
|
2.7
|
24.7
|
1.0
|
O
|
A:ALA22
|
2.8
|
31.4
|
1.0
|
C
|
A:ALA22
|
3.3
|
30.5
|
1.0
|
CA
|
A:ALA22
|
3.5
|
27.4
|
1.0
|
MG
|
A:MG1167
|
3.6
|
40.6
|
1.0
|
O
|
A:HOH2012
|
3.6
|
52.0
|
1.0
|
C
|
A:ASN21
|
3.7
|
25.2
|
1.0
|
C
|
A:THR24
|
3.8
|
32.1
|
1.0
|
N
|
A:ALA22
|
4.0
|
25.8
|
1.0
|
N
|
A:THR24
|
4.2
|
27.9
|
1.0
|
O
|
A:HOH2107
|
4.2
|
34.0
|
1.0
|
N
|
A:LEU23
|
4.4
|
29.0
|
1.0
|
O
|
A:HOH2009
|
4.4
|
43.5
|
1.0
|
OE1
|
A:GLU26
|
4.5
|
71.2
|
1.0
|
C
|
A:LEU23
|
4.5
|
29.7
|
1.0
|
CA
|
A:THR24
|
4.6
|
27.4
|
1.0
|
O
|
A:HOH2015
|
4.7
|
52.4
|
1.0
|
CB
|
A:ALA22
|
4.8
|
28.8
|
1.0
|
N
|
A:GLY25
|
4.8
|
35.9
|
1.0
|
CA
|
A:GLY25
|
4.9
|
43.4
|
1.0
|
O
|
A:LEU23
|
5.0
|
29.1
|
1.0
|
CA
|
A:LEU23
|
5.0
|
24.3
|
1.0
|
|
Magnesium binding site 3 out
of 3 in 2wjh
Go back to
Magnesium Binding Sites List in 2wjh
Magnesium binding site 3 out
of 3 in the Structure and Function of the Feob G-Domain From Methanococcus Jannaschii
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Structure and Function of the Feob G-Domain From Methanococcus Jannaschii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1167
b:91.0
occ:1.00
|
O
|
B:THR24
|
2.7
|
65.5
|
1.0
|
O
|
B:ASN21
|
2.7
|
42.9
|
1.0
|
OE2
|
B:GLU26
|
2.7
|
0.9
|
1.0
|
O
|
B:HOH2008
|
2.8
|
58.5
|
1.0
|
O
|
B:HOH2007
|
2.9
|
69.6
|
1.0
|
O
|
B:GLY25
|
3.2
|
89.3
|
1.0
|
C
|
B:GLY25
|
3.3
|
89.5
|
1.0
|
N
|
B:GLU26
|
3.6
|
96.0
|
1.0
|
CD
|
B:GLU26
|
3.7
|
0.7
|
1.0
|
C
|
B:THR24
|
3.7
|
65.0
|
1.0
|
O
|
B:HOH2009
|
3.8
|
58.8
|
1.0
|
C
|
B:ASN21
|
3.8
|
42.0
|
1.0
|
CA
|
B:GLY25
|
3.9
|
82.1
|
1.0
|
CA
|
B:GLU26
|
3.9
|
0.2
|
1.0
|
O
|
B:HOH2010
|
4.1
|
54.9
|
1.0
|
CG
|
B:GLU26
|
4.1
|
0.4
|
1.0
|
N
|
B:GLY25
|
4.2
|
72.8
|
1.0
|
OG1
|
B:THR24
|
4.4
|
39.1
|
1.0
|
CA
|
B:ASN21
|
4.5
|
41.3
|
1.0
|
CB
|
B:GLU26
|
4.6
|
0.5
|
1.0
|
OE1
|
B:GLU26
|
4.7
|
0.8
|
1.0
|
N
|
B:ALA22
|
4.8
|
41.5
|
1.0
|
CA
|
B:THR24
|
4.8
|
57.4
|
1.0
|
CB
|
B:ASN21
|
4.9
|
42.3
|
1.0
|
CA
|
B:ALA22
|
4.9
|
38.5
|
1.0
|
|
Reference:
S.Koester,
M.Wehner,
C.Herrmann,
W.Kuehlbrandt,
O.Yildiz.
Structure and Function of the Feob G-Domain From Methanococcus Jannaschii J.Mol.Biol. V. 392 405 2009.
ISSN: ISSN 0022-2836
PubMed: 19615379
DOI: 10.1016/J.JMB.2009.07.020
Page generated: Wed Aug 14 06:07:17 2024
|