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Magnesium in PDB 9ev3: Corynebacterium Glutamicum Pyruvate:Quinone Oxidoreductase (Pqo) Purified From Bacteria Grown in Acetate Minimal Medium

Enzymatic activity of Corynebacterium Glutamicum Pyruvate:Quinone Oxidoreductase (Pqo) Purified From Bacteria Grown in Acetate Minimal Medium

All present enzymatic activity of Corynebacterium Glutamicum Pyruvate:Quinone Oxidoreductase (Pqo) Purified From Bacteria Grown in Acetate Minimal Medium:
1.2.5.1;

Protein crystallography data

The structure of Corynebacterium Glutamicum Pyruvate:Quinone Oxidoreductase (Pqo) Purified From Bacteria Grown in Acetate Minimal Medium, PDB code: 9ev3 was solved by C.Da Silva Lameira, S.Muenssinger, L.Yang, B.J.Eikmanns, M.Bellinzoni, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.67 / 1.22
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 68.044, 119.072, 155.305, 90, 90, 90
R / Rfree (%) 17.6 / 19.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Corynebacterium Glutamicum Pyruvate:Quinone Oxidoreductase (Pqo) Purified From Bacteria Grown in Acetate Minimal Medium (pdb code 9ev3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Corynebacterium Glutamicum Pyruvate:Quinone Oxidoreductase (Pqo) Purified From Bacteria Grown in Acetate Minimal Medium, PDB code: 9ev3:

Magnesium binding site 1 out of 1 in 9ev3

Go back to Magnesium Binding Sites List in 9ev3
Magnesium binding site 1 out of 1 in the Corynebacterium Glutamicum Pyruvate:Quinone Oxidoreductase (Pqo) Purified From Bacteria Grown in Acetate Minimal Medium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Corynebacterium Glutamicum Pyruvate:Quinone Oxidoreductase (Pqo) Purified From Bacteria Grown in Acetate Minimal Medium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg603

b:13.6
occ:0.50
 O A:SER465 2.1 25.2 1.0
O A:HOH720 2.2 25.1 1.0
OD1 A:ASP436 2.3 19.3 1.0
O2B A:TPP602 2.3 17.9 0.5
O2A A:TPP602 2.5 16.3 0.5
OD1 A:ASN463 2.5 25.6 1.0
CG A:ASP436 3.3 18.2 1.0
C A:SER465 3.4 24.5 1.0
PB A:TPP602 3.5 19.6 0.5
CG A:ASN463 3.6 27.1 1.0
PA A:TPP602 3.7 16.9 0.5
O3A A:TPP602 3.8 16.6 0.5
OD2 A:ASP436 3.8 21.0 1.0
O A:HOH721 3.9 37.1 1.0
N A:SER465 3.9 23.0 1.0
N A:ASP436 4.0 13.3 1.0
O1B A:TPP602 4.0 22.9 0.5
ND2 A:ASN463 4.0 31.0 1.0
CA A:SER465 4.2 23.7 1.0
N A:GLY467 4.2 23.7 1.0
O A:PHE461 4.2 17.7 1.0
N A:GLY437 4.3 12.9 1.0
O A:HOH957 4.3 36.2 1.0
N A:LEU466 4.4 23.5 1.0
O7 A:TPP602 4.5 21.2 0.5
CB A:ASP436 4.5 15.8 1.0
N A:ASN463 4.5 19.4 1.0
CA A:LEU466 4.6 23.9 1.0
CB A:SER465 4.7 26.7 1.0
CA A:ASP436 4.7 13.2 1.0
O3B A:TPP602 4.7 16.0 0.5
CA A:GLY435 4.8 14.6 1.0
C A:GLY435 4.8 14.3 1.0
N A:SER464 4.8 20.6 1.0
CB A:ASN463 4.8 24.3 1.0
O1A A:TPP602 4.9 12.8 0.5
C A:LEU466 4.9 23.9 1.0
C A:ASN463 5.0 21.7 1.0
CA A:ASN463 5.0 21.0 1.0

Reference:

C.Da Silva Lameira, S.Munssinger, L.Yang, B.J.Eikmanns, M.Bellinzoni. Corynebacterium Glutamicum Pyruvate:Quinone Oxidoreductase: An Enigmatic Metabolic Enzyme with Unusual Structural Features. Febs J. 2024.
ISSN: ISSN 1742-464X
PubMed: 39080980
DOI: 10.1111/FEBS.17232
Page generated: Sat Aug 16 01:32:24 2025

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