Atomistry » Magnesium » PDB 4g7h-4gni » 4gd3
Atomistry »
  Magnesium »
    PDB 4g7h-4gni »
      4gd3 »

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

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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy