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Magnesium in PDB 6pa3: E. Coli L-Asparaginase II Double Mutant (T12V,K162T) in Complex with L-Asn at pH 7.0

Enzymatic activity of E. Coli L-Asparaginase II Double Mutant (T12V,K162T) in Complex with L-Asn at pH 7.0

All present enzymatic activity of E. Coli L-Asparaginase II Double Mutant (T12V,K162T) in Complex with L-Asn at pH 7.0:
3.5.1.1;

Protein crystallography data

The structure of E. Coli L-Asparaginase II Double Mutant (T12V,K162T) in Complex with L-Asn at pH 7.0, PDB code: 6pa3 was solved by J.Lubkowski, A.Wlodawer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.65
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 152.852, 62.990, 141.293, 90.00, 117.83, 90.00
R / Rfree (%) 14.9 / 18.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the E. Coli L-Asparaginase II Double Mutant (T12V,K162T) in Complex with L-Asn at pH 7.0 (pdb code 6pa3). 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 E. Coli L-Asparaginase II Double Mutant (T12V,K162T) in Complex with L-Asn at pH 7.0, PDB code: 6pa3:

Magnesium binding site 1 out of 1 in 6pa3

Go back to Magnesium Binding Sites List in 6pa3
Magnesium binding site 1 out of 1 in the E. Coli L-Asparaginase II Double Mutant (T12V,K162T) in Complex with L-Asn at pH 7.0


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli L-Asparaginase II Double Mutant (T12V,K162T) in Complex with L-Asn at pH 7.0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg405

b:13.2
occ:1.00
NE2 A:HIS-2 2.0 29.7 1.0
O A:HOH667 2.2 38.6 1.0
NE2 A:HIS-4 2.2 32.4 1.0
N1 A:IMD404 2.3 32.8 1.0
N1 A:IMD403 2.6 44.7 1.0
N1 A:IMD402 2.9 40.6 1.0
CE1 A:HIS-2 3.0 30.8 1.0
C5 A:IMD402 3.1 42.8 1.0
CD2 A:HIS-2 3.1 32.0 1.0
CE1 A:HIS-4 3.1 35.1 1.0
C2 A:IMD404 3.1 35.2 1.0
CD2 A:HIS-4 3.2 32.7 1.0
C5 A:IMD404 3.4 33.6 1.0
C2 A:IMD403 3.5 44.9 1.0
C5 A:IMD403 3.6 44.6 1.0
ND1 A:HIS-2 4.1 31.5 1.0
CG A:HIS-2 4.2 31.1 1.0
ND1 A:HIS-4 4.2 34.8 1.0
C2 A:IMD402 4.2 42.6 1.0
CG A:HIS-4 4.3 31.6 1.0
N3 A:IMD404 4.4 33.9 1.0
C4 A:IMD402 4.4 43.3 1.0
C4 A:IMD404 4.5 34.0 1.0
N3 A:IMD403 4.6 45.5 1.0
C4 A:IMD403 4.7 44.4 1.0
O A:HOH697 4.9 36.1 1.0
N3 A:IMD402 5.0 45.6 1.0

Reference:

J.Lubkowski, A.Wlodawer. Geometric Considerations Support the Double-Displacement Catalytic Mechanism of L-Asparaginase. Protein Sci. V. 28 1850 2019.
ISSN: ESSN 1469-896X
PubMed: 31423681
DOI: 10.1002/PRO.3709
Page generated: Tue Oct 1 14:00:14 2024

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