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Aluminium in PDB 6hdj: R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed Aluminium Tetrafluoride and Beta-G6P to 1.2 A.

Enzymatic activity of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed Aluminium Tetrafluoride and Beta-G6P to 1.2 A.

All present enzymatic activity of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed Aluminium Tetrafluoride and Beta-G6P to 1.2 A.:
5.4.2.6;

Protein crystallography data

The structure of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed Aluminium Tetrafluoride and Beta-G6P to 1.2 A., PDB code: 6hdj was solved by A.J.Robertson, C.Bisson, J.P.Waltho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.10 / 1.16
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 104.210, 37.220, 54.220, 90.00, 90.00, 90.00
R / Rfree (%) 14.3 / 16.6

Other elements in 6hdj:

The structure of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed Aluminium Tetrafluoride and Beta-G6P to 1.2 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 R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed Aluminium Tetrafluoride and Beta-G6P to 1.2 A. (pdb code 6hdj). 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 R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed Aluminium Tetrafluoride and Beta-G6P to 1.2 A., PDB code: 6hdj:

Aluminium binding site 1 out of 1 in 6hdj

Go back to Aluminium Binding Sites List in 6hdj
Aluminium binding site 1 out of 1 in the R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed Aluminium Tetrafluoride and Beta-G6P to 1.2 A.


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of R49K Variant of Beta-Phosphoglucomutase From Lactococcus Lactis Complexed Aluminium Tetrafluoride and Beta-G6P to 1.2 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al305

b:8.8
occ:1.00
 AL A:ALF305 0.0 8.8 1.0
F3 A:ALF305 1.7 9.9 1.0
F2 A:ALF305 1.8 9.4 1.0
F1 A:ALF305 1.8 8.9 1.0
F4 A:ALF305 1.8 8.6 1.0
OD1 A:ASP8 1.9 8.4 1.0
O1 A:BG6306 2.0 7.8 1.0
CG A:ASP8 3.0 8.3 1.0
C1 A:BG6306 3.1 8.2 1.0
OD2 A:ASP8 3.4 9.3 1.0
MG A:MG304 3.5 8.6 1.0
O A:HOH426 3.5 9.9 1.0
O2 A:BG6306 3.6 8.4 1.0
NZ A:LYS145 3.6 11.6 1.0
OG A:SER114 3.8 9.6 1.0
OD2 A:ASP10 3.9 9.5 1.0
C2 A:BG6306 3.9 8.0 1.0
N A:ASP10 4.0 7.8 1.0
N A:LEU9 4.0 8.3 1.0
O5 A:BG6306 4.1 8.7 1.0
CB A:ASP8 4.3 8.7 1.0
N A:ALA115 4.3 9.3 1.0
CB A:ASP10 4.4 7.7 1.0
CA A:SER114 4.5 10.6 1.0
CG A:ASP10 4.5 9.1 1.0
CB A:SER114 4.5 10.1 1.0
O A:ASP10 4.6 8.9 1.0
CA A:ASP8 4.7 8.2 1.0
OE2 A:GLU169 4.7 11.6 1.0
CA A:ASP10 4.7 8.0 1.0
O A:HOH455 4.7 9.8 1.0
C A:LEU9 4.8 8.1 1.0
CA A:GLY46 4.8 10.2 1.0
CA A:LEU9 4.8 8.2 1.0
CE A:LYS145 4.8 12.3 1.0
C A:ASP8 4.8 8.3 1.0
CB A:ALA115 4.9 12.1 1.0
C A:SER114 5.0 9.9 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: Sun Jul 6 21:58:54 2025

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