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Magnesium in PDB 2yj3: Conformational Changes in the Catalytic Domain of the Cpx- Atpase Copb-B Upon Nucleotide Binding

Enzymatic activity of Conformational Changes in the Catalytic Domain of the Cpx- Atpase Copb-B Upon Nucleotide Binding

All present enzymatic activity of Conformational Changes in the Catalytic Domain of the Cpx- Atpase Copb-B Upon Nucleotide Binding:
3.6.1.36; 3.6.3.10;

Protein crystallography data

The structure of Conformational Changes in the Catalytic Domain of the Cpx- Atpase Copb-B Upon Nucleotide Binding, PDB code: 2yj3 was solved by C.Voellmecke, C.Schlicker, M.Luebben, E.Hofmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.464 / 2.20
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 71.980, 52.590, 68.790, 90.00, 90.00, 90.00
R / Rfree (%) 21.93 / 28.36

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Conformational Changes in the Catalytic Domain of the Cpx- Atpase Copb-B Upon Nucleotide Binding (pdb code 2yj3). 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 Conformational Changes in the Catalytic Domain of the Cpx- Atpase Copb-B Upon Nucleotide Binding, PDB code: 2yj3:

Magnesium binding site 1 out of 1 in 2yj3

Go back to Magnesium Binding Sites List in 2yj3
Magnesium binding site 1 out of 1 in the Conformational Changes in the Catalytic Domain of the Cpx- Atpase Copb-B Upon Nucleotide Binding


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Conformational Changes in the Catalytic Domain of the Cpx- Atpase Copb-B Upon Nucleotide Binding within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1636

b:45.3
occ:1.00
 O A:ALA455 2.6 35.9 1.0
O A:HOH2004 2.9 35.6 1.0
O A:HOH2010 3.0 45.2 1.0
N A:VAL428 3.1 35.7 1.0
C A:ALA455 3.4 37.2 1.0
CA A:ILE427 3.6 39.8 1.0
CA A:ALA455 3.6 32.6 1.0
CG2 A:VAL428 3.7 26.0 1.0
CB A:ALA455 3.8 39.4 1.0
CB A:TYR459 3.8 26.4 1.0
CB A:VAL428 3.8 31.6 1.0
C A:ILE427 3.8 40.3 1.0
N A:TYR459 3.9 29.5 1.0
CB A:ILE427 4.0 42.0 1.0
CA A:VAL428 4.1 34.6 1.0
CA A:TYR459 4.3 27.0 1.0
CG2 A:ILE427 4.3 51.5 1.0
O A:PRO426 4.3 46.9 1.0
CB A:LYS458 4.4 37.2 1.0
N A:ILE456 4.6 32.4 1.0
CG A:LYS458 4.8 43.0 1.0
N A:ILE427 4.8 37.6 1.0
C A:LYS458 4.8 38.1 1.0
O A:VAL428 4.9 37.8 1.0
CD A:LYS458 4.9 49.9 1.0
CG A:TYR459 4.9 32.0 1.0
C A:PRO426 5.0 42.0 1.0
C A:VAL428 5.0 39.3 1.0

Reference:

C.Voellmecke, C.Schlicker, M.Luebben, E.Hofmann. Conformational Changes in the Catalytic Domain of the Cpx-Atpase Copb-B Upon Nucleotide Binding To Be Published.
Page generated: Sun Aug 10 16:43:34 2025

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