Magnesium in PDB 6q93: Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii
Enzymatic activity of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii
All present enzymatic activity of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii:
1.18.6.1;
Protein crystallography data
The structure of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii, PDB code: 6q93
was solved by
M.Rohde,
S.Gerhardt,
O.Einsle,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
49.10 /
2.20
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
94.573,
176.857,
354.225,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20 /
21.5
|
Other elements in 6q93:
The structure of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii
(pdb code 6q93). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 10 binding sites of Magnesium where determined in the
Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii, PDB code: 6q93:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Magnesium binding site 1 out
of 10 in 6q93
Go back to
Magnesium Binding Sites List in 6q93
Magnesium binding site 1 out
of 10 in the Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1003
b:42.9
occ:1.00
|
OG
|
A:SER17
|
1.9
|
41.7
|
1.0
|
O3B
|
A:ADP1002
|
2.0
|
39.3
|
1.0
|
O
|
A:HOH1104
|
2.0
|
42.0
|
1.0
|
O
|
A:HOH1120
|
2.1
|
44.5
|
1.0
|
O
|
A:HOH1135
|
2.1
|
39.2
|
1.0
|
O
|
A:HOH1121
|
2.2
|
45.3
|
1.0
|
CB
|
A:SER17
|
3.1
|
35.0
|
1.0
|
PB
|
A:ADP1002
|
3.3
|
43.5
|
1.0
|
O1B
|
A:ADP1002
|
3.5
|
45.7
|
1.0
|
OD2
|
A:ASP40
|
3.8
|
46.9
|
1.0
|
N
|
A:SER17
|
3.9
|
33.5
|
1.0
|
OD1
|
A:ASP44
|
3.9
|
49.2
|
1.0
|
OD2
|
A:ASP126
|
4.0
|
49.4
|
1.0
|
CA
|
A:SER17
|
4.0
|
33.3
|
1.0
|
O1A
|
A:ADP1002
|
4.1
|
43.6
|
1.0
|
OD1
|
A:ASP126
|
4.2
|
36.3
|
1.0
|
OG
|
A:SER45
|
4.2
|
48.5
|
1.0
|
O3A
|
A:ADP1002
|
4.3
|
40.3
|
1.0
|
O2B
|
A:ADP1002
|
4.3
|
43.4
|
1.0
|
CG
|
A:ASP126
|
4.5
|
39.9
|
1.0
|
CG
|
A:ASP40
|
4.5
|
47.0
|
1.0
|
PA
|
A:ADP1002
|
4.6
|
43.0
|
1.0
|
O
|
A:HOH1136
|
4.6
|
48.8
|
1.0
|
O2A
|
A:ADP1002
|
4.7
|
44.1
|
1.0
|
CB
|
A:LYS16
|
4.8
|
36.8
|
1.0
|
CE
|
A:LYS16
|
4.9
|
34.9
|
1.0
|
CG
|
A:ASP44
|
4.9
|
52.5
|
1.0
|
CB
|
A:ASP40
|
4.9
|
38.1
|
1.0
|
C
|
A:LYS16
|
4.9
|
38.0
|
1.0
|
|
Magnesium binding site 2 out
of 10 in 6q93
Go back to
Magnesium Binding Sites List in 6q93
Magnesium binding site 2 out
of 10 in the Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg302
b:87.5
occ:1.00
|
O
|
B:HOH405
|
2.0
|
94.9
|
1.0
|
OG
|
B:SER17
|
2.1
|
88.2
|
1.0
|
O
|
B:HOH406
|
2.3
|
68.6
|
1.0
|
O3B
|
B:ADP301
|
2.4
|
75.2
|
1.0
|
O
|
B:HOH402
|
2.6
|
61.1
|
1.0
|
CB
|
B:SER17
|
3.2
|
79.2
|
1.0
|
OD2
|
B:ASP40
|
3.6
|
80.3
|
1.0
|
PB
|
B:ADP301
|
3.7
|
76.2
|
1.0
|
OD1
|
B:ASP44
|
3.7
|
93.0
|
1.0
|
O2B
|
B:ADP301
|
3.9
|
76.3
|
1.0
|
OG
|
B:SER45
|
4.0
|
93.2
|
1.0
|
N
|
B:SER17
|
4.0
|
73.1
|
1.0
|
OD2
|
B:ASP126
|
4.1
|
91.3
|
1.0
|
CG
|
B:ASP40
|
4.1
|
71.4
|
1.0
|
CA
|
B:SER17
|
4.2
|
74.8
|
1.0
|
CB
|
B:ASP40
|
4.4
|
62.7
|
1.0
|
OD1
|
B:ASP126
|
4.5
|
82.4
|
1.0
|
O2A
|
B:ADP301
|
4.6
|
70.1
|
1.0
|
O1B
|
B:ADP301
|
4.7
|
71.7
|
1.0
|
O3A
|
B:ADP301
|
4.7
|
76.9
|
1.0
|
CG
|
B:ASP126
|
4.7
|
82.7
|
1.0
|
CB
|
B:SER45
|
4.7
|
81.8
|
1.0
|
CA
|
B:SER45
|
4.8
|
79.0
|
1.0
|
CB
|
B:LYS16
|
4.8
|
70.0
|
1.0
|
N
|
B:SER45
|
4.8
|
78.8
|
1.0
|
OD1
|
B:ASP40
|
4.9
|
69.7
|
1.0
|
CG
|
B:ASP44
|
4.9
|
93.1
|
1.0
|
PA
|
B:ADP301
|
5.0
|
72.7
|
1.0
|
CE
|
B:LYS16
|
5.0
|
81.1
|
1.0
|
|
Magnesium binding site 3 out
of 10 in 6q93
Go back to
Magnesium Binding Sites List in 6q93
Magnesium binding site 3 out
of 10 in the Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1003
b:47.1
occ:1.00
|
O
|
C:HOH1102
|
2.0
|
36.6
|
1.0
|
O
|
C:HOH1103
|
2.1
|
36.7
|
1.0
|
O3B
|
C:ADP1002
|
2.1
|
41.2
|
1.0
|
OG
|
C:SER17
|
2.1
|
42.5
|
1.0
|
O
|
C:HOH1118
|
2.1
|
38.0
|
1.0
|
O
|
C:HOH1121
|
2.2
|
40.6
|
1.0
|
CB
|
C:SER17
|
3.2
|
41.3
|
1.0
|
PB
|
C:ADP1002
|
3.3
|
41.6
|
1.0
|
O2B
|
C:ADP1002
|
3.5
|
40.7
|
1.0
|
OD2
|
C:ASP40
|
3.6
|
47.2
|
1.0
|
OD1
|
C:ASP44
|
3.8
|
60.0
|
1.0
|
N
|
C:SER17
|
4.0
|
37.5
|
1.0
|
OD2
|
C:ASP126
|
4.1
|
55.9
|
1.0
|
OG
|
C:SER45
|
4.2
|
47.3
|
1.0
|
CA
|
C:SER17
|
4.2
|
37.6
|
1.0
|
O2A
|
C:ADP1002
|
4.2
|
42.1
|
1.0
|
CG
|
C:ASP40
|
4.3
|
45.0
|
1.0
|
OD1
|
C:ASP126
|
4.3
|
42.2
|
1.0
|
O3A
|
C:ADP1002
|
4.3
|
41.5
|
1.0
|
O1B
|
C:ADP1002
|
4.3
|
43.2
|
1.0
|
CG
|
C:ASP126
|
4.6
|
45.9
|
1.0
|
PA
|
C:ADP1002
|
4.7
|
43.5
|
1.0
|
CB
|
C:ASP40
|
4.7
|
38.4
|
1.0
|
O1A
|
C:ADP1002
|
4.9
|
40.2
|
1.0
|
CE
|
C:LYS16
|
4.9
|
35.3
|
1.0
|
CG
|
C:ASP44
|
4.9
|
58.0
|
1.0
|
CD
|
C:LYS42
|
4.9
|
50.9
|
1.0
|
CB
|
C:LYS16
|
4.9
|
38.3
|
1.0
|
|
Magnesium binding site 4 out
of 10 in 6q93
Go back to
Magnesium Binding Sites List in 6q93
Magnesium binding site 4 out
of 10 in the Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1004
b:94.6
occ:1.00
|
OE1
|
C:GLU113
|
3.1
|
0.8
|
1.0
|
OE2
|
C:GLU113
|
3.2
|
1.0
|
1.0
|
CD
|
C:GLU113
|
3.5
|
0.8
|
1.0
|
O
|
C:GLU69
|
3.6
|
99.8
|
1.0
|
O
|
C:LEU71
|
3.6
|
77.7
|
1.0
|
OE1
|
C:GLU72
|
3.9
|
0.3
|
1.0
|
C
|
C:GLU69
|
4.5
|
97.3
|
1.0
|
CD
|
C:GLU72
|
4.6
|
0.7
|
1.0
|
C
|
C:LEU71
|
4.8
|
76.8
|
1.0
|
CG
|
C:GLU113
|
4.8
|
87.7
|
1.0
|
OE2
|
C:GLU72
|
4.9
|
0.2
|
1.0
|
|
Magnesium binding site 5 out
of 10 in 6q93
Go back to
Magnesium Binding Sites List in 6q93
Magnesium binding site 5 out
of 10 in the Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg302
b:53.9
occ:1.00
|
OG
|
D:SER17
|
1.9
|
56.2
|
1.0
|
O
|
D:HOH408
|
2.0
|
45.0
|
1.0
|
O3B
|
D:ADP301
|
2.1
|
52.2
|
1.0
|
O
|
D:HOH409
|
2.2
|
47.6
|
1.0
|
O
|
D:HOH403
|
2.2
|
41.0
|
1.0
|
O
|
D:HOH406
|
2.2
|
41.0
|
1.0
|
CB
|
D:SER17
|
3.1
|
55.9
|
1.0
|
PB
|
D:ADP301
|
3.4
|
52.8
|
1.0
|
O1B
|
D:ADP301
|
3.6
|
53.8
|
1.0
|
OD1
|
D:ASP44
|
3.8
|
65.3
|
1.0
|
OD2
|
D:ASP40
|
3.8
|
62.0
|
1.0
|
N
|
D:SER17
|
3.9
|
54.7
|
1.0
|
OD2
|
D:ASP126
|
4.0
|
64.2
|
1.0
|
CA
|
D:SER17
|
4.1
|
54.4
|
1.0
|
O1A
|
D:ADP301
|
4.2
|
58.9
|
1.0
|
OD1
|
D:ASP126
|
4.2
|
54.1
|
1.0
|
O3A
|
D:ADP301
|
4.3
|
56.3
|
1.0
|
O2B
|
D:ADP301
|
4.4
|
51.3
|
1.0
|
OG
|
D:SER45
|
4.4
|
59.5
|
1.0
|
CG
|
D:ASP40
|
4.5
|
58.6
|
1.0
|
CG
|
D:ASP126
|
4.5
|
55.5
|
1.0
|
PA
|
D:ADP301
|
4.6
|
55.9
|
1.0
|
O2A
|
D:ADP301
|
4.7
|
52.3
|
1.0
|
CG
|
D:ASP44
|
4.9
|
66.6
|
1.0
|
CB
|
D:LYS16
|
4.9
|
54.5
|
1.0
|
CB
|
D:ASP40
|
4.9
|
47.3
|
1.0
|
C
|
D:LYS16
|
5.0
|
58.0
|
1.0
|
CE
|
D:LYS16
|
5.0
|
46.7
|
1.0
|
|
Magnesium binding site 6 out
of 10 in 6q93
Go back to
Magnesium Binding Sites List in 6q93
Magnesium binding site 6 out
of 10 in the Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg1003
b:74.5
occ:1.00
|
O
|
E:HOH1108
|
2.0
|
66.8
|
1.0
|
O3B
|
E:ADP1002
|
2.1
|
69.6
|
1.0
|
O
|
E:HOH1105
|
2.2
|
62.0
|
1.0
|
O
|
E:HOH1101
|
2.3
|
58.3
|
1.0
|
OG
|
E:SER17
|
2.7
|
71.3
|
1.0
|
O2B
|
E:ADP1002
|
3.0
|
63.5
|
1.0
|
PB
|
E:ADP1002
|
3.1
|
67.0
|
1.0
|
OD2
|
E:ASP40
|
3.3
|
64.4
|
1.0
|
CB
|
E:SER17
|
3.7
|
65.2
|
1.0
|
OD1
|
E:ASP44
|
3.8
|
81.6
|
1.0
|
CG
|
E:ASP40
|
4.1
|
61.4
|
1.0
|
O3A
|
E:ADP1002
|
4.1
|
65.7
|
1.0
|
O2A
|
E:ADP1002
|
4.2
|
59.6
|
1.0
|
O1B
|
E:ADP1002
|
4.2
|
63.8
|
1.0
|
NZ
|
E:LYS16
|
4.4
|
92.0
|
1.0
|
N
|
E:SER17
|
4.5
|
60.0
|
1.0
|
CD
|
E:LYS42
|
4.5
|
79.3
|
1.0
|
OG
|
E:SER45
|
4.6
|
75.2
|
1.0
|
PA
|
E:ADP1002
|
4.6
|
61.0
|
1.0
|
CB
|
E:ASP40
|
4.7
|
54.0
|
1.0
|
CB
|
E:LYS42
|
4.7
|
60.3
|
1.0
|
CA
|
E:SER17
|
4.7
|
61.2
|
1.0
|
OD1
|
E:ASP40
|
4.7
|
63.3
|
1.0
|
OD1
|
E:ASP126
|
4.7
|
67.4
|
1.0
|
OD2
|
E:ASP126
|
4.7
|
72.6
|
1.0
|
CG
|
E:ASP44
|
5.0
|
82.2
|
1.0
|
O1A
|
E:ADP1002
|
5.0
|
60.4
|
1.0
|
CE
|
E:LYS16
|
5.0
|
67.0
|
1.0
|
|
Magnesium binding site 7 out
of 10 in 6q93
Go back to
Magnesium Binding Sites List in 6q93
Magnesium binding site 7 out
of 10 in the Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg302
b:50.8
occ:1.00
|
O
|
F:HOH402
|
2.0
|
46.3
|
1.0
|
O
|
F:HOH420
|
2.0
|
44.3
|
1.0
|
O3B
|
F:ADP301
|
2.1
|
45.1
|
1.0
|
O
|
F:HOH407
|
2.1
|
43.8
|
1.0
|
OG
|
F:SER17
|
2.2
|
46.7
|
1.0
|
O
|
F:HOH423
|
2.5
|
52.6
|
1.0
|
PB
|
F:ADP301
|
3.3
|
47.9
|
1.0
|
CB
|
F:SER17
|
3.4
|
40.8
|
1.0
|
O1B
|
F:ADP301
|
3.4
|
47.2
|
1.0
|
OD2
|
F:ASP40
|
3.5
|
49.5
|
1.0
|
OD1
|
F:ASP44
|
3.9
|
57.8
|
1.0
|
N
|
F:SER17
|
4.1
|
40.5
|
1.0
|
OD2
|
F:ASP126
|
4.2
|
48.9
|
1.0
|
OG
|
F:SER45
|
4.2
|
48.4
|
1.0
|
CG
|
F:ASP40
|
4.3
|
48.0
|
1.0
|
OD1
|
F:ASP126
|
4.3
|
44.0
|
1.0
|
O2B
|
F:ADP301
|
4.3
|
47.9
|
1.0
|
O1A
|
F:ADP301
|
4.3
|
49.1
|
1.0
|
CA
|
F:SER17
|
4.3
|
39.7
|
1.0
|
O3A
|
F:ADP301
|
4.3
|
47.2
|
1.0
|
O
|
F:HOH438
|
4.5
|
53.0
|
1.0
|
CG
|
F:ASP126
|
4.6
|
43.0
|
1.0
|
CB
|
F:ASP40
|
4.7
|
38.0
|
1.0
|
PA
|
F:ADP301
|
4.7
|
48.9
|
1.0
|
CE
|
F:LYS16
|
4.8
|
40.3
|
1.0
|
O2A
|
F:ADP301
|
4.9
|
49.3
|
1.0
|
CB
|
F:LYS16
|
4.9
|
41.6
|
1.0
|
NZ
|
F:LYS16
|
4.9
|
50.0
|
1.0
|
O
|
F:HOH411
|
5.0
|
47.2
|
1.0
|
CG
|
F:ASP44
|
5.0
|
60.4
|
1.0
|
CD
|
F:LYS42
|
5.0
|
67.4
|
1.0
|
|
Magnesium binding site 8 out
of 10 in 6q93
Go back to
Magnesium Binding Sites List in 6q93
Magnesium binding site 8 out
of 10 in the Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg303
b:95.1
occ:1.00
|
O
|
F:GLU69
|
3.2
|
61.3
|
1.0
|
OE2
|
F:GLU113
|
3.6
|
87.1
|
1.0
|
O
|
F:LEU71
|
3.7
|
55.1
|
1.0
|
OE1
|
F:GLU72
|
3.9
|
89.4
|
1.0
|
C
|
F:GLU69
|
4.3
|
60.0
|
1.0
|
CD
|
F:GLU113
|
4.3
|
85.0
|
1.0
|
OE1
|
F:GLU113
|
4.4
|
83.7
|
1.0
|
CD
|
F:GLU72
|
4.8
|
91.8
|
1.0
|
C
|
F:LEU71
|
4.8
|
53.4
|
1.0
|
|
Magnesium binding site 9 out
of 10 in 6q93
Go back to
Magnesium Binding Sites List in 6q93
Magnesium binding site 9 out
of 10 in the Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 9 of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg1003
b:54.0
occ:1.00
|
O
|
G:HOH1111
|
2.1
|
52.4
|
1.0
|
O3B
|
G:ADP1002
|
2.1
|
51.2
|
1.0
|
O
|
G:HOH1119
|
2.1
|
43.8
|
1.0
|
O
|
G:HOH1117
|
2.1
|
44.3
|
1.0
|
OG
|
G:SER17
|
2.1
|
53.5
|
1.0
|
O
|
G:HOH1114
|
2.2
|
47.9
|
1.0
|
CB
|
G:SER17
|
3.2
|
53.0
|
1.0
|
PB
|
G:ADP1002
|
3.3
|
55.2
|
1.0
|
O1B
|
G:ADP1002
|
3.5
|
52.9
|
1.0
|
OD2
|
G:ASP40
|
3.7
|
55.8
|
1.0
|
OD1
|
G:ASP44
|
3.7
|
70.0
|
1.0
|
OD2
|
G:ASP126
|
4.1
|
58.0
|
1.0
|
N
|
G:SER17
|
4.1
|
52.2
|
1.0
|
O1A
|
G:ADP1002
|
4.1
|
63.2
|
1.0
|
OG
|
G:SER45
|
4.2
|
66.2
|
1.0
|
CA
|
G:SER17
|
4.3
|
52.2
|
1.0
|
O3A
|
G:ADP1002
|
4.3
|
59.0
|
1.0
|
O2B
|
G:ADP1002
|
4.4
|
51.8
|
1.0
|
CG
|
G:ASP40
|
4.4
|
54.3
|
1.0
|
OD1
|
G:ASP126
|
4.5
|
47.8
|
1.0
|
PA
|
G:ADP1002
|
4.6
|
60.0
|
1.0
|
CG
|
G:ASP126
|
4.7
|
50.7
|
1.0
|
O2A
|
G:ADP1002
|
4.8
|
56.7
|
1.0
|
CB
|
G:ASP40
|
4.8
|
47.6
|
1.0
|
CG
|
G:ASP44
|
4.8
|
71.2
|
1.0
|
CE
|
G:LYS16
|
4.9
|
50.8
|
1.0
|
CD
|
G:LYS42
|
4.9
|
61.0
|
1.0
|
CB
|
G:LYS16
|
5.0
|
51.5
|
1.0
|
|
Magnesium binding site 10 out
of 10 in 6q93
Go back to
Magnesium Binding Sites List in 6q93
Magnesium binding site 10 out
of 10 in the Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 10 of Mgadp-Bound Fe Protein of Vanadium Nitrogenase From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg302
b:48.8
occ:1.00
|
O
|
H:HOH403
|
1.9
|
37.5
|
1.0
|
O
|
H:HOH416
|
2.0
|
36.0
|
1.0
|
O
|
H:HOH406
|
2.0
|
39.5
|
1.0
|
O3B
|
H:ADP301
|
2.1
|
36.9
|
1.0
|
OG
|
H:SER17
|
2.1
|
41.2
|
1.0
|
O
|
H:HOH422
|
2.2
|
40.4
|
1.0
|
CB
|
H:SER17
|
3.3
|
40.4
|
1.0
|
PB
|
H:ADP301
|
3.4
|
42.2
|
1.0
|
OD2
|
H:ASP40
|
3.6
|
49.4
|
1.0
|
O2B
|
H:ADP301
|
3.6
|
42.2
|
1.0
|
OD1
|
H:ASP44
|
3.8
|
57.6
|
1.0
|
OD2
|
H:ASP126
|
4.0
|
53.0
|
1.0
|
N
|
H:SER17
|
4.0
|
40.4
|
1.0
|
OG
|
H:SER45
|
4.1
|
51.3
|
1.0
|
CA
|
H:SER17
|
4.3
|
39.3
|
1.0
|
CG
|
H:ASP40
|
4.3
|
48.7
|
1.0
|
OD1
|
H:ASP126
|
4.3
|
40.1
|
1.0
|
O2A
|
H:ADP301
|
4.3
|
44.7
|
1.0
|
O3A
|
H:ADP301
|
4.4
|
43.6
|
1.0
|
O1B
|
H:ADP301
|
4.4
|
44.4
|
1.0
|
CG
|
H:ASP126
|
4.5
|
44.2
|
1.0
|
CB
|
H:ASP40
|
4.6
|
42.6
|
1.0
|
PA
|
H:ADP301
|
4.7
|
44.0
|
1.0
|
O
|
H:HOH411
|
4.8
|
46.1
|
1.0
|
CE
|
H:LYS16
|
4.8
|
36.6
|
1.0
|
CB
|
H:LYS16
|
4.8
|
43.9
|
1.0
|
O1A
|
H:ADP301
|
4.9
|
40.9
|
1.0
|
CG
|
H:ASP44
|
4.9
|
57.0
|
1.0
|
CD
|
H:LYS42
|
5.0
|
53.5
|
1.0
|
|
Reference:
M.Rohde,
C.Trncik,
D.Sippel,
S.Gerhardt,
O.Einsle.
Crystal Structure of Vnfh, the Iron Protein Component of Vanadium Nitrogenase. J. Biol. Inorg. Chem. V. 23 1049 2018.
ISSN: ESSN 1432-1327
PubMed: 30141094
DOI: 10.1007/S00775-018-1602-4
Page generated: Tue Oct 1 15:25:47 2024
|