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Aluminium in PDB 5o6r: Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride

Enzymatic activity of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride

All present enzymatic activity of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride:
5.4.2.6;

Protein crystallography data

The structure of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride, PDB code: 5o6r was solved by M.W.Bowler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.36
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.300, 54.900, 107.560, 90.00, 90.00, 90.00
R / Rfree (%) 11.5 / 14.9

Other elements in 5o6r:

The structure of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Magnesium (Mg) 2 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride (pdb code 5o6r). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride, PDB code: 5o6r:

Aluminium binding site 1 out of 1 in 5o6r

Go back to Aluminium Binding Sites List in 5o6r
Aluminium binding site 1 out of 1 in the Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Structure of Beta-Phosphoglucomutase D10N Mutant in Complex with Glucose-1-Phosphate and Aluminium Tetrafluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al303

b:6.7
occ:0.80
 AL A:ALF303 0.0 6.7 0.8
F1 A:ALF303 1.8 6.5 0.8
F3 A:ALF303 1.8 7.0 0.8
F2 A:ALF303 1.8 6.3 0.8
O A:HOH407 1.8 10.1 1.0
F4 A:ALF303 1.8 8.7 0.8
OD1 A:ASP8 1.9 6.8 1.0
CG A:ASP8 3.0 6.8 1.0
OD2 A:ASP8 3.4 6.9 1.0
MG A:MG301 3.5 8.2 1.0
NZ A:LYS145 3.6 7.9 1.0
O A:HOH443 3.6 9.5 1.0
O A:HOH656 3.8 11.1 1.0
O6 A:XGP302 3.9 11.3 1.0
OG A:SER114 3.9 7.6 1.0
N A:ASN10 4.0 6.2 1.0
N A:LEU9 4.1 6.9 1.0
CA A:GLY46 4.3 8.5 1.0
N A:GLY46 4.3 8.0 1.0
CB A:ASP8 4.3 6.4 1.0
N A:ALA115 4.4 7.0 1.0
O A:ASN10 4.5 8.2 1.0
O A:HOH576 4.5 9.5 1.0
CA A:SER114 4.5 6.8 1.0
C6 A:XGP302 4.5 10.2 1.0
CB A:ASN10 4.6 7.1 1.0
CB A:SER114 4.6 6.7 1.0
CE A:LYS145 4.6 7.6 1.0
OE2 A:GLU169 4.6 10.4 1.0
CA A:ASP8 4.7 6.5 1.0
CA A:ASN10 4.8 6.9 1.0
CA A:LEU9 4.8 6.9 0.5
C A:LEU9 4.9 6.6 1.0
CB A:LEU9 4.9 7.8 0.5
ND2 A:ASN10 4.9 8.7 1.0
CA A:LEU9 4.9 7.1 0.5
C A:ASP8 4.9 6.6 1.0

Reference:

L.A.Johnson, A.J.Robertson, N.J.Baxter, C.R.Trevitt, C.Bisson, Y.Jin, H.P.Wood, A.M.Hounslow, M.J.Cliff, G.M.Blackburn, M.W.Bowler, J.P.Waltho. Van Der Waals Contact Between Nucleophile and Transferring Phosphorus Is Insufficient to Achieve Enzyme Transition-State Architecture Acs Catalysis 2018.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.8B01612
Page generated: Wed Jul 10 09:51:15 2024

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