Magnesium in PDB 4ue2: Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase
Enzymatic activity of Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase
All present enzymatic activity of Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase:
1.12.2.1;
Protein crystallography data
The structure of Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase, PDB code: 4ue2
was solved by
A.Volbeda,
L.Martin,
P.-P.Liebgott,
J.C.Fontecilla-Camps,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.91 /
2.02
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
65.090,
99.650,
184.170,
90.00,
91.16,
90.00
|
R / Rfree (%)
|
16.381 /
19.135
|
Other elements in 4ue2:
The structure of Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase
(pdb code 4ue2). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase, PDB code: 4ue2:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 4ue2
Go back to
Magnesium Binding Sites List in 4ue2
Magnesium binding site 1 out
of 4 in the Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
Q:Mg1553
b:12.2
occ:1.00
|
O
|
Q:HOH2289
|
2.0
|
11.7
|
1.0
|
O
|
Q:HOH2043
|
2.1
|
12.4
|
1.0
|
O
|
Q:HOH2044
|
2.1
|
11.3
|
1.0
|
O
|
Q:LEU495
|
2.1
|
12.2
|
1.0
|
OE2
|
Q:GLU53
|
2.1
|
12.8
|
1.0
|
NE2
|
Q:HIS549
|
2.2
|
12.4
|
1.0
|
CE1
|
Q:HIS549
|
3.1
|
12.0
|
1.0
|
CD
|
Q:GLU53
|
3.1
|
13.4
|
1.0
|
C
|
Q:LEU495
|
3.3
|
12.4
|
1.0
|
CD2
|
Q:HIS549
|
3.3
|
11.5
|
1.0
|
OE1
|
Q:GLU53
|
3.4
|
13.3
|
1.0
|
N
|
Q:LEU495
|
3.7
|
12.8
|
1.0
|
CA
|
Q:LEU495
|
3.9
|
13.1
|
1.0
|
OE1
|
Q:GLN494
|
4.0
|
11.9
|
1.0
|
OE1
|
Q:GLU334
|
4.1
|
12.6
|
1.0
|
OE2
|
Q:GLU334
|
4.1
|
11.6
|
1.0
|
CB
|
Q:LEU495
|
4.2
|
13.5
|
1.0
|
O
|
Q:HOH2323
|
4.3
|
14.3
|
1.0
|
NZ
|
Q:LYS372
|
4.3
|
13.7
|
1.0
|
ND1
|
Q:HIS549
|
4.3
|
11.3
|
1.0
|
O
|
Q:HOH2295
|
4.3
|
11.7
|
1.0
|
N
|
Q:VAL496
|
4.4
|
11.8
|
1.0
|
CG
|
Q:GLU53
|
4.4
|
13.0
|
1.0
|
CG
|
Q:HIS549
|
4.4
|
11.7
|
1.0
|
CD
|
Q:LYS372
|
4.6
|
13.0
|
1.0
|
CD
|
Q:GLU334
|
4.6
|
12.5
|
1.0
|
CE
|
Q:LYS372
|
4.7
|
13.3
|
1.0
|
CA
|
Q:VAL496
|
4.7
|
11.5
|
1.0
|
C
|
Q:GLN494
|
4.7
|
12.7
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 4ue2
Go back to
Magnesium Binding Sites List in 4ue2
Magnesium binding site 2 out
of 4 in the Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
R:Mg1553
b:16.6
occ:1.00
|
O
|
R:HOH2044
|
2.0
|
15.9
|
1.0
|
O
|
R:HOH2045
|
2.0
|
15.3
|
1.0
|
O
|
R:HOH2266
|
2.0
|
14.7
|
1.0
|
O
|
R:LEU495
|
2.1
|
16.1
|
1.0
|
OE2
|
R:GLU53
|
2.1
|
16.6
|
1.0
|
NE2
|
R:HIS549
|
2.2
|
15.8
|
1.0
|
CE1
|
R:HIS549
|
3.0
|
14.9
|
1.0
|
CD
|
R:GLU53
|
3.1
|
17.1
|
1.0
|
C
|
R:LEU495
|
3.2
|
15.6
|
1.0
|
CD2
|
R:HIS549
|
3.3
|
15.6
|
1.0
|
OE1
|
R:GLU53
|
3.4
|
16.2
|
1.0
|
N
|
R:LEU495
|
3.7
|
16.1
|
1.0
|
CA
|
R:LEU495
|
3.9
|
15.9
|
1.0
|
OE1
|
R:GLN494
|
4.1
|
17.7
|
1.0
|
OE2
|
R:GLU334
|
4.1
|
14.1
|
1.0
|
CB
|
R:LEU495
|
4.2
|
16.3
|
1.0
|
OE1
|
R:GLU334
|
4.2
|
15.3
|
1.0
|
ND1
|
R:HIS549
|
4.2
|
14.8
|
1.0
|
NZ
|
R:LYS372
|
4.3
|
15.1
|
1.0
|
N
|
R:VAL496
|
4.3
|
14.7
|
1.0
|
O
|
R:HOH2305
|
4.3
|
16.6
|
1.0
|
O
|
R:HOH2275
|
4.3
|
18.8
|
1.0
|
CG
|
R:HIS549
|
4.4
|
14.9
|
1.0
|
CG
|
R:GLU53
|
4.4
|
16.4
|
1.0
|
CD
|
R:LYS372
|
4.5
|
14.7
|
1.0
|
CD
|
R:GLU334
|
4.6
|
15.2
|
1.0
|
CA
|
R:VAL496
|
4.7
|
14.2
|
1.0
|
C
|
R:GLN494
|
4.7
|
16.6
|
1.0
|
CE
|
R:LYS372
|
4.7
|
15.2
|
1.0
|
CA
|
R:GLN494
|
5.0
|
17.0
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 4ue2
Go back to
Magnesium Binding Sites List in 4ue2
Magnesium binding site 3 out
of 4 in the Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
R:Mg1560
b:46.0
occ:1.00
|
O
|
R:HOH2158
|
2.2
|
15.4
|
1.0
|
O
|
B:HOH2075
|
2.4
|
26.3
|
1.0
|
OD1
|
R:ASN181
|
2.5
|
16.8
|
1.0
|
CG
|
R:ASN181
|
3.6
|
16.9
|
1.0
|
N
|
R:ASN181
|
3.9
|
16.5
|
1.0
|
O
|
B:HOH2022
|
4.0
|
37.9
|
1.0
|
CA
|
R:ASN181
|
4.0
|
16.8
|
1.0
|
CB
|
R:ASN181
|
4.4
|
16.4
|
1.0
|
CD1
|
R:LEU185
|
4.6
|
16.5
|
1.0
|
ND2
|
R:ASN181
|
4.6
|
16.3
|
1.0
|
O2
|
R:GOL1562
|
4.6
|
24.4
|
1.0
|
OE1
|
B:GLN62
|
4.8
|
41.1
|
1.0
|
CG2
|
R:THR180
|
4.8
|
17.6
|
1.0
|
NE2
|
B:GLN62
|
4.9
|
37.3
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 4ue2
Go back to
Magnesium Binding Sites List in 4ue2
Magnesium binding site 4 out
of 4 in the Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase
 Mono view
 Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Structure of Air-Treated Anaerobically Purified D. Fructosovorans Nife-Hydrogenase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
S:Mg1553
b:18.8
occ:1.00
|
O
|
S:HOH2032
|
2.0
|
18.8
|
1.0
|
O
|
S:HOH2031
|
2.0
|
18.3
|
1.0
|
O
|
S:HOH2206
|
2.0
|
19.3
|
1.0
|
OE2
|
S:GLU53
|
2.1
|
17.1
|
1.0
|
O
|
S:LEU495
|
2.1
|
19.1
|
1.0
|
NE2
|
S:HIS549
|
2.1
|
17.2
|
1.0
|
CE1
|
S:HIS549
|
3.0
|
16.7
|
1.0
|
CD
|
S:GLU53
|
3.1
|
17.2
|
1.0
|
CD2
|
S:HIS549
|
3.2
|
16.6
|
1.0
|
C
|
S:LEU495
|
3.3
|
19.4
|
1.0
|
OE1
|
S:GLU53
|
3.4
|
16.6
|
1.0
|
N
|
S:LEU495
|
3.7
|
19.2
|
1.0
|
CA
|
S:LEU495
|
4.0
|
18.9
|
1.0
|
OE2
|
S:GLU334
|
4.1
|
20.9
|
1.0
|
OE1
|
S:GLN494
|
4.1
|
20.3
|
1.0
|
OE1
|
S:GLU334
|
4.1
|
20.7
|
1.0
|
ND1
|
S:HIS549
|
4.2
|
16.6
|
1.0
|
NZ
|
S:LYS372
|
4.2
|
21.3
|
1.0
|
CB
|
S:LEU495
|
4.2
|
19.6
|
1.0
|
O
|
S:HOH2213
|
4.3
|
22.8
|
1.0
|
O
|
S:HOH2239
|
4.3
|
19.5
|
1.0
|
CG
|
S:HIS549
|
4.3
|
16.3
|
1.0
|
N
|
S:VAL496
|
4.4
|
18.6
|
1.0
|
CG
|
S:GLU53
|
4.4
|
16.6
|
1.0
|
CD
|
S:GLU334
|
4.5
|
21.9
|
1.0
|
CD
|
S:LYS372
|
4.6
|
20.7
|
1.0
|
CE
|
S:LYS372
|
4.7
|
20.8
|
1.0
|
CA
|
S:VAL496
|
4.7
|
18.8
|
1.0
|
C
|
S:GLN494
|
4.8
|
19.8
|
1.0
|
|
Reference:
A.Volbeda,
L.Martin,
P.-P.Liebgott,
A.L.De Lacey,
J.C.Fontecilla-Camps.
[Nife]-Hydrogenases Revisited: Nickel-Carboxamido Bond Formation in A Variant with Accrued O2-Tolerance and A Tentative Re-Interpretation of Ni-Si States. Metallomics 2015.
ISSN: ESSN 1756-591X
PubMed: 25780984
DOI: 10.1039/C4MT00309H
Page generated: Tue Aug 20 04:38:54 2024
|