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Magnesium in PDB 2yjg: Structure of the Lactate Racemase Apoprotein From Thermoanaerobacterium Thermosaccharolyticum

Enzymatic activity of Structure of the Lactate Racemase Apoprotein From Thermoanaerobacterium Thermosaccharolyticum

All present enzymatic activity of Structure of the Lactate Racemase Apoprotein From Thermoanaerobacterium Thermosaccharolyticum:
5.1.2.1;

Protein crystallography data

The structure of Structure of the Lactate Racemase Apoprotein From Thermoanaerobacterium Thermosaccharolyticum, PDB code: 2yjg was solved by J.P.Declercq, B.Desguin, P.Soumillion, P.Hols, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 114.96 / 1.80
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.410, 223.250, 46.140, 90.00, 90.00, 90.00
R / Rfree (%) 18.2 / 22.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Lactate Racemase Apoprotein From Thermoanaerobacterium Thermosaccharolyticum (pdb code 2yjg). 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 Structure of the Lactate Racemase Apoprotein From Thermoanaerobacterium Thermosaccharolyticum, PDB code: 2yjg:

Magnesium binding site 1 out of 1 in 2yjg

Go back to Magnesium Binding Sites List in 2yjg
Magnesium binding site 1 out of 1 in the Structure of the Lactate Racemase Apoprotein From Thermoanaerobacterium Thermosaccharolyticum


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Lactate Racemase Apoprotein From Thermoanaerobacterium Thermosaccharolyticum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1427

b:15.5
occ:1.00
 O A:GLU128 2.3 16.8 1.0
O B:GLU128 2.3 14.0 1.0
O B:VAL125 2.4 13.9 1.0
O A:VAL125 2.4 15.3 1.0
O A:GLU126 2.5 18.2 1.0
O B:GLU126 2.7 15.9 1.0
C A:GLU126 3.2 16.0 1.0
C B:GLU126 3.3 16.3 1.0
C A:GLU128 3.5 15.4 1.0
C B:GLU128 3.5 15.1 1.0
C B:VAL125 3.5 16.2 1.0
C A:VAL125 3.5 16.4 1.0
CA A:GLU126 3.6 16.4 1.0
CA B:GLU126 3.7 17.1 1.0
N B:GLU126 4.0 16.8 1.0
N A:GLU126 4.1 16.7 1.0
N B:GLU128 4.1 14.8 1.0
N A:GLU128 4.2 13.7 1.0
N A:ASN127 4.3 15.3 1.0
N B:ASN127 4.3 15.5 1.0
N A:GLN129 4.3 15.3 1.0
N B:GLN129 4.4 14.2 1.0
CA B:GLN129 4.4 15.2 1.0
CA A:GLN129 4.4 15.6 1.0
CA B:GLU128 4.4 16.2 1.0
CA A:GLU128 4.4 14.0 1.0
N B:PHE130 4.6 16.0 1.0
C A:ASN127 4.6 16.0 1.0
C B:ASN127 4.6 15.5 1.0
N A:PHE130 4.6 15.7 1.0
CA B:VAL125 4.8 17.5 1.0
CA A:VAL125 4.8 16.5 1.0
O B:LEU124 4.9 17.4 1.0
CA A:ASN127 4.9 15.4 1.0
O A:LEU124 5.0 16.2 1.0
CA B:ASN127 5.0 14.8 1.0

Reference:

B.Desguin, P.Goffin, E.Viaene, M.Kleerebezem, V.Martin-Diaconescu, M.J.Maroney, J.Declercq, P.Soumillion, P.Hols. Lactate Racemase Is A Nickel-Dependent Enzyme Activated By A Widespread Maturation System. Nat.Commun. V. 5 3615 2014.
ISSN: ESSN 2041-1723
PubMed: 24710389
DOI: 10.1038/NCOMMS4615
Page generated: Mon Dec 14 07:49:04 2020

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