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Manganese in PDB 7b1s: Crystal Structure of the Ethyl-Coenzyme M Reductase From Candidatus Ethanoperedens Thermophilum at 0.994-A Resolution

Enzymatic activity of Crystal Structure of the Ethyl-Coenzyme M Reductase From Candidatus Ethanoperedens Thermophilum at 0.994-A Resolution

All present enzymatic activity of Crystal Structure of the Ethyl-Coenzyme M Reductase From Candidatus Ethanoperedens Thermophilum at 0.994-A Resolution:
2.8.4.1;

Protein crystallography data

The structure of Crystal Structure of the Ethyl-Coenzyme M Reductase From Candidatus Ethanoperedens Thermophilum at 0.994-A Resolution, PDB code: 7b1s was solved by T.Wagner, O.N.Lemaire, S.Engilberge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.76 / 0.99
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 83.736, 146.927, 113.128, 90, 106.98, 90
R / Rfree (%) 11.2 / 12.8

Other elements in 7b1s:

The structure of Crystal Structure of the Ethyl-Coenzyme M Reductase From Candidatus Ethanoperedens Thermophilum at 0.994-A Resolution also contains other interesting chemical elements:

Potassium (K) 4 atoms
Chlorine (Cl) 6 atoms
Nickel (Ni) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Ethyl-Coenzyme M Reductase From Candidatus Ethanoperedens Thermophilum at 0.994-A Resolution (pdb code 7b1s). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of the Ethyl-Coenzyme M Reductase From Candidatus Ethanoperedens Thermophilum at 0.994-A Resolution, PDB code: 7b1s:

Manganese binding site 1 out of 1 in 7b1s

Go back to Manganese Binding Sites List in 7b1s
Manganese binding site 1 out of 1 in the Crystal Structure of the Ethyl-Coenzyme M Reductase From Candidatus Ethanoperedens Thermophilum at 0.994-A Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Ethyl-Coenzyme M Reductase From Candidatus Ethanoperedens Thermophilum at 0.994-A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn603

b:8.5
occ:1.00
 OD1 D:ASP589 2.0 10.2 1.0
OD1 A:ASP589 2.0 9.4 1.0
NE2 D:HIS595 2.2 13.5 0.5
O A:HOH1569 2.2 10.1 1.0
O D:HOH1405 2.2 10.2 1.0
NE2 A:HIS595 2.2 12.9 0.5
NE2 D:HIS595 2.2 13.2 0.5
NE2 A:HIS595 2.3 15.7 0.5
CG A:ASP589 3.0 9.0 1.0
CG D:ASP589 3.0 9.8 1.0
CE1 D:HIS595 3.1 13.1 0.5
CE1 A:HIS595 3.1 12.8 0.5
CE1 D:HIS595 3.1 12.4 0.5
CE1 A:HIS595 3.1 15.7 0.5
CD2 D:HIS595 3.2 14.5 0.5
CD2 A:HIS595 3.2 14.3 0.5
CD2 D:HIS595 3.3 14.0 0.5
OD2 A:ASP589 3.3 11.0 1.0
CD2 A:HIS595 3.3 16.8 0.5
OD2 D:ASP589 3.4 10.8 1.0
ND1 D:HIS595 4.2 13.4 0.5
ND1 D:HIS595 4.3 12.7 0.5
ND1 A:HIS595 4.3 13.3 0.5
CG D:HIS595 4.3 14.6 0.5
ND1 A:HIS595 4.3 16.3 0.5
CB D:ASP589 4.3 8.4 1.0
CB A:ASP589 4.3 8.1 1.0
CG A:HIS595 4.3 15.1 0.5
CG D:HIS595 4.4 14.4 0.5
CG A:HIS595 4.4 17.8 0.5
O D:HOH1227 4.5 29.9 0.8
OE1 A:GLU587 4.6 7.3 1.0
OE1 D:GLU587 4.6 7.4 1.0
CA D:ASP589 4.8 7.0 1.0
CD1 D:ILE592 4.8 8.9 1.0
CA A:ASP589 4.8 6.6 1.0
CD1 A:ILE592 4.9 9.1 1.0
O D:HOH1679 5.0 34.5 1.0

Reference:

C.J.Hahn, O.N.Lemaire, J.Kahnt, S.Engilberge, G.Wegener, T.Wagner. Crystal Structure of A Key Enzyme For Anaerobic Ethane Activation. Science V. 373 118 2021.
ISSN: ESSN 1095-9203
PubMed: 34210888
DOI: 10.1126/SCIENCE.ABG1765
Page generated: Sun Oct 6 08:06:37 2024

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