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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:

Nickel (Ni) 4 atoms
Iron (Fe) 54 atoms
Chlorine (Cl) 10 atoms

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

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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: Mon Dec 14 16:15:43 2020

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