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Aluminium in PDB 6h8w: Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A.

Enzymatic activity of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A.

All present enzymatic activity of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A.:
5.4.2.6;

Protein crystallography data

The structure of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A., PDB code: 6h8w was solved by A.J.Robertson, C.Bisson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.44 / 1.98
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.440, 53.710, 80.880, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 24.8

Other elements in 6h8w:

The structure of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A. also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Magnesium (Mg) 1 atom

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A. (pdb code 6h8w). 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 Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A., PDB code: 6h8w:

Aluminium binding site 1 out of 1 in 6h8w

Go back to Aluminium Binding Sites List in 6h8w
Aluminium binding site 1 out of 1 in the Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A.


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al302

b:30.4
occ:1.00
 AL A:ALF302 0.0 30.4 1.0
F4 A:ALF302 1.8 28.4 1.0
F3 A:ALF302 1.8 29.1 1.0
F1 A:ALF302 1.8 29.2 1.0
F2 A:ALF302 1.8 29.5 1.0
O A:HOH524 1.9 28.6 1.0
OD1 A:ASP8 2.0 20.9 1.0
CG A:ASP8 2.9 21.1 1.0
OD2 A:ASP8 3.1 22.5 1.0
NZ A:LYS145 3.6 21.4 1.0
MG A:MG301 3.6 33.3 1.0
O A:HOH440 3.7 22.4 1.0
O A:HOH403 4.0 35.0 1.0
OG A:SER114 4.1 15.0 1.0
N A:ASP10 4.1 18.0 0.2
N A:ASP10 4.1 19.4 0.8
N A:LEU9 4.2 16.3 1.0
CB A:ASP8 4.3 19.4 1.0
CB A:ASP10 4.4 17.4 0.2
N A:ALA115 4.4 17.0 1.0
O A:ASP10 4.4 19.1 0.8
O A:ASP10 4.4 18.1 0.2
OE2 A:GLU169 4.5 19.7 1.0
O A:HOH450 4.6 27.5 1.0
CB A:ASP10 4.6 23.1 0.8
CA A:SER114 4.6 15.9 1.0
CE A:LYS145 4.7 22.0 1.0
CA A:ASP10 4.7 17.8 0.2
CB A:SER114 4.7 15.3 1.0
CA A:ASP10 4.7 20.5 0.8
CG A:ASP10 4.8 16.7 0.2
CA A:ASP8 4.8 18.5 1.0
C A:LEU9 4.9 18.4 1.0
C A:ASP8 5.0 17.1 1.0

Reference:

A.J.Robertson, C.Bisson, J.P.Waltho. Transition State of Phospho-Enzyme Hydrolysis in Beta-Phosphoglucomutase. To Be Published.
Page generated: Wed Jul 10 09:52:45 2024

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