Magnesium in PDB 4gd3: Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B
Enzymatic activity of Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B
All present enzymatic activity of Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B:
1.12.99.6;
Protein crystallography data
The structure of Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B, PDB code: 4gd3
was solved by
A.Volbeda,
J.C.Fontecilla-Camps,
C.Darnault,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
25.00 /
3.30
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
126.000,
165.300,
212.800,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20 /
23.6
|
Other elements in 4gd3:
The structure of Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B
(pdb code 4gd3). 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 E. Coli Hydrogenase-1 in Complex with Cytochrome B, PDB code: 4gd3:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 4gd3
Go back to
Magnesium Binding Sites List in 4gd3
Magnesium binding site 1 out
of 4 in the Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
L:Mg603
b:99.4
occ:1.00
|
O
|
L:HOH701
|
2.0
|
98.6
|
1.0
|
O
|
L:HOH703
|
2.0
|
0.3
|
1.0
|
O
|
L:HOH702
|
2.0
|
96.2
|
1.0
|
OE1
|
L:GLU57
|
2.1
|
0.3
|
1.0
|
O
|
L:CYS528
|
2.1
|
97.8
|
1.0
|
NE2
|
L:HIS582
|
2.5
|
0.1
|
1.0
|
CD
|
L:GLU57
|
3.2
|
0.2
|
1.0
|
C
|
L:CYS528
|
3.3
|
96.9
|
1.0
|
CD2
|
L:HIS582
|
3.5
|
97.6
|
1.0
|
CE1
|
L:HIS582
|
3.5
|
99.7
|
1.0
|
OE2
|
L:GLU57
|
3.6
|
0.4
|
1.0
|
N
|
L:CYS528
|
3.8
|
97.4
|
1.0
|
OE1
|
L:GLN527
|
3.9
|
0.8
|
1.0
|
CA
|
L:CYS528
|
3.9
|
96.4
|
1.0
|
OE2
|
L:GLU347
|
4.0
|
0.0
|
1.0
|
OE1
|
L:GLU347
|
4.1
|
0.4
|
1.0
|
CB
|
L:CYS528
|
4.2
|
94.7
|
1.0
|
CD
|
L:LYS399
|
4.2
|
98.9
|
1.0
|
N
|
L:VAL529
|
4.4
|
97.4
|
1.0
|
CG
|
L:GLU57
|
4.5
|
98.0
|
1.0
|
CD
|
L:GLU347
|
4.5
|
1.0
|
1.0
|
CE
|
L:LYS399
|
4.5
|
0.6
|
1.0
|
NZ
|
L:LYS399
|
4.6
|
0.5
|
1.0
|
CG
|
L:HIS582
|
4.6
|
94.4
|
1.0
|
ND1
|
L:HIS582
|
4.6
|
95.3
|
1.0
|
CA
|
L:VAL529
|
4.7
|
98.5
|
1.0
|
OG1
|
L:THR370
|
4.8
|
0.4
|
1.0
|
CG2
|
L:VAL529
|
4.9
|
0.3
|
1.0
|
C
|
L:GLN527
|
4.9
|
97.8
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 4gd3
Go back to
Magnesium Binding Sites List in 4gd3
Magnesium binding site 2 out
of 4 in the Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
M:Mg604
b:95.6
occ:1.00
|
O
|
M:HOH702
|
2.0
|
92.3
|
1.0
|
O
|
M:HOH701
|
2.0
|
96.9
|
1.0
|
O
|
M:HOH703
|
2.0
|
96.9
|
1.0
|
O
|
M:CYS528
|
2.1
|
91.0
|
1.0
|
OE1
|
M:GLU57
|
2.1
|
97.3
|
1.0
|
NE2
|
M:HIS582
|
2.5
|
98.2
|
1.0
|
CD
|
M:GLU57
|
3.2
|
99.6
|
1.0
|
C
|
M:CYS528
|
3.3
|
89.0
|
1.0
|
CD2
|
M:HIS582
|
3.4
|
96.0
|
1.0
|
CE1
|
M:HIS582
|
3.5
|
97.1
|
1.0
|
OE2
|
M:GLU57
|
3.6
|
0.4
|
1.0
|
N
|
M:CYS528
|
3.8
|
89.5
|
1.0
|
CA
|
M:CYS528
|
3.9
|
88.7
|
1.0
|
OE1
|
M:GLN527
|
4.0
|
0.8
|
1.0
|
OE2
|
M:GLU347
|
4.0
|
0.0
|
1.0
|
CB
|
M:CYS528
|
4.1
|
88.2
|
1.0
|
OE1
|
M:GLU347
|
4.2
|
0.1
|
1.0
|
CD
|
M:LYS399
|
4.2
|
97.7
|
1.0
|
N
|
M:VAL529
|
4.4
|
88.2
|
1.0
|
CE
|
M:LYS399
|
4.5
|
0.0
|
1.0
|
CG
|
M:GLU57
|
4.5
|
94.9
|
1.0
|
CD
|
M:GLU347
|
4.5
|
0.2
|
1.0
|
NZ
|
M:LYS399
|
4.6
|
0.6
|
1.0
|
CG
|
M:HIS582
|
4.6
|
93.6
|
1.0
|
ND1
|
M:HIS582
|
4.6
|
93.7
|
1.0
|
OG1
|
M:THR370
|
4.8
|
0.2
|
1.0
|
CA
|
M:VAL529
|
4.8
|
89.5
|
1.0
|
CG2
|
M:VAL529
|
5.0
|
90.5
|
1.0
|
C
|
M:GLN527
|
5.0
|
88.8
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 4gd3
Go back to
Magnesium Binding Sites List in 4gd3
Magnesium binding site 3 out
of 4 in the Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Mg603
b:87.6
occ:1.00
|
O
|
J:HOH702
|
2.0
|
85.0
|
1.0
|
O
|
J:HOH701
|
2.0
|
87.0
|
1.0
|
O
|
J:HOH703
|
2.0
|
89.4
|
1.0
|
OE1
|
J:GLU57
|
2.1
|
90.1
|
1.0
|
O
|
J:CYS528
|
2.1
|
87.5
|
1.0
|
NE2
|
J:HIS582
|
2.5
|
89.5
|
1.0
|
CD
|
J:GLU57
|
3.1
|
92.2
|
1.0
|
C
|
J:CYS528
|
3.2
|
86.9
|
1.0
|
CD2
|
J:HIS582
|
3.4
|
87.5
|
1.0
|
CE1
|
J:HIS582
|
3.5
|
88.9
|
1.0
|
OE2
|
J:GLU57
|
3.5
|
93.8
|
1.0
|
N
|
J:CYS528
|
3.7
|
87.7
|
1.0
|
CA
|
J:CYS528
|
3.8
|
87.3
|
1.0
|
OE1
|
J:GLN527
|
3.9
|
95.4
|
1.0
|
OE2
|
J:GLU347
|
4.1
|
99.1
|
1.0
|
CB
|
J:CYS528
|
4.1
|
85.8
|
1.0
|
OE1
|
J:GLU347
|
4.2
|
0.3
|
1.0
|
CD
|
J:LYS399
|
4.3
|
85.9
|
1.0
|
N
|
J:VAL529
|
4.4
|
87.2
|
1.0
|
CG
|
J:GLU57
|
4.4
|
88.6
|
1.0
|
CE
|
J:LYS399
|
4.6
|
88.6
|
1.0
|
CG
|
J:HIS582
|
4.6
|
84.6
|
1.0
|
ND1
|
J:HIS582
|
4.6
|
85.3
|
1.0
|
NZ
|
J:LYS399
|
4.6
|
92.5
|
1.0
|
CD
|
J:GLU347
|
4.6
|
0.6
|
1.0
|
CA
|
J:VAL529
|
4.8
|
88.1
|
1.0
|
OG1
|
J:THR370
|
4.8
|
90.7
|
1.0
|
C
|
J:GLN527
|
4.9
|
88.0
|
1.0
|
CG2
|
J:VAL529
|
5.0
|
89.3
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 4gd3
Go back to
Magnesium Binding Sites List in 4gd3
Magnesium binding site 4 out
of 4 in the Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Structure of E. Coli Hydrogenase-1 in Complex with Cytochrome B within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
K:Mg604
b:97.0
occ:1.00
|
O
|
K:HOH702
|
2.0
|
94.0
|
1.0
|
O
|
K:HOH703
|
2.0
|
98.5
|
1.0
|
O
|
K:HOH701
|
2.0
|
97.4
|
1.0
|
O
|
K:CYS528
|
2.1
|
94.1
|
1.0
|
OE1
|
K:GLU57
|
2.1
|
98.9
|
1.0
|
NE2
|
K:HIS582
|
2.5
|
0.3
|
1.0
|
CD
|
K:GLU57
|
3.1
|
0.3
|
1.0
|
C
|
K:CYS528
|
3.2
|
93.6
|
1.0
|
CD2
|
K:HIS582
|
3.4
|
98.3
|
1.0
|
CE1
|
K:HIS582
|
3.5
|
99.2
|
1.0
|
OE2
|
K:GLU57
|
3.5
|
0.9
|
1.0
|
N
|
K:CYS528
|
3.7
|
93.7
|
1.0
|
CA
|
K:CYS528
|
3.8
|
93.7
|
1.0
|
OE1
|
K:GLN527
|
3.9
|
0.3
|
1.0
|
CB
|
K:CYS528
|
4.1
|
92.9
|
1.0
|
OE2
|
K:GLU347
|
4.1
|
1.0
|
1.0
|
CD
|
K:LYS399
|
4.2
|
96.5
|
1.0
|
OE1
|
K:GLU347
|
4.3
|
0.7
|
1.0
|
N
|
K:VAL529
|
4.3
|
93.1
|
1.0
|
CG
|
K:GLU57
|
4.4
|
97.3
|
1.0
|
CE
|
K:LYS399
|
4.5
|
99.3
|
1.0
|
NZ
|
K:LYS399
|
4.5
|
0.4
|
1.0
|
CG
|
K:HIS582
|
4.6
|
96.3
|
1.0
|
CD
|
K:GLU347
|
4.6
|
0.5
|
1.0
|
ND1
|
K:HIS582
|
4.6
|
96.3
|
1.0
|
CA
|
K:VAL529
|
4.8
|
93.7
|
1.0
|
OG1
|
K:THR370
|
4.8
|
0.3
|
1.0
|
C
|
K:GLN527
|
4.9
|
93.2
|
1.0
|
CG2
|
K:VAL529
|
5.0
|
95.1
|
1.0
|
|
Reference:
A.Volbeda,
C.Darnault,
A.Parkin,
F.Sargent,
F.A.Armstrong,
J.C.Fontecilla-Camps.
Crystal Structure of the O(2)-Tolerant Membrane-Bound Hydrogenase 1 From Escherichia Coli in Complex with Its Cognate Cytochrome B. Structure V. 21 184 2013.
ISSN: ISSN 0969-2126
PubMed: 23260654
DOI: 10.1016/J.STR.2012.11.010
Page generated: Fri Aug 16 15:29:53 2024
|