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Calcium in PDB 8ax3: Structure of Recombinant Human Beta-Glucocerebrosidase in Complex with L-Carbaxylosyl Fluoride

Enzymatic activity of Structure of Recombinant Human Beta-Glucocerebrosidase in Complex with L-Carbaxylosyl Fluoride

All present enzymatic activity of Structure of Recombinant Human Beta-Glucocerebrosidase in Complex with L-Carbaxylosyl Fluoride:
3.2.1.104; 3.2.1.45;

Protein crystallography data

The structure of Structure of Recombinant Human Beta-Glucocerebrosidase in Complex with L-Carbaxylosyl Fluoride, PDB code: 8ax3 was solved by R.J.Rowland, G.J.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 51.82 / 1.59
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 52.92, 155.984, 68.036, 90, 101.96, 90
R / Rfree (%) 18.2 / 21.3

Other elements in 8ax3:

The structure of Structure of Recombinant Human Beta-Glucocerebrosidase in Complex with L-Carbaxylosyl Fluoride also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Sodium (Na) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Recombinant Human Beta-Glucocerebrosidase in Complex with L-Carbaxylosyl Fluoride (pdb code 8ax3). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of Recombinant Human Beta-Glucocerebrosidase in Complex with L-Carbaxylosyl Fluoride, PDB code: 8ax3:

Calcium binding site 1 out of 1 in 8ax3

Go back to Calcium Binding Sites List in 8ax3
Calcium binding site 1 out of 1 in the Structure of Recombinant Human Beta-Glucocerebrosidase in Complex with L-Carbaxylosyl Fluoride


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Recombinant Human Beta-Glucocerebrosidase in Complex with L-Carbaxylosyl Fluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca532

b:55.0
occ:1.00
 H3 B:OD0516 3.0 19.6 1.0
H12 B:EDO509 3.1 41.0 1.0
OE1 B:GLU235 3.1 15.4 1.0
HO1 B:EDO509 3.1 46.0 0.0
O1 B:EDO509 3.4 45.3 1.0
HE21 B:GLN284 3.6 18.4 1.0
OE2 B:GLU235 3.6 14.1 1.0
H4 B:OD0516 3.6 19.5 1.0
C2 B:OD0516 3.7 19.8 1.0
HH B:TYR244 3.7 20.1 0.0
C1 B:EDO509 3.7 40.7 1.0
CD B:GLU235 3.8 14.5 1.0
HO2 B:EDO509 3.9 33.9 1.0
NE2 B:GLN284 4.0 18.9 1.0
C3 B:OD0516 4.0 19.4 1.0
HE22 B:GLN284 4.0 18.4 1.0
HB2 B:TYR313 4.0 14.3 1.0
HD2 B:TYR313 4.1 14.5 1.0
CD2 B:TYR313 4.2 14.6 1.0
CG B:TYR313 4.3 14.1 1.0
HB3 B:TYR313 4.3 14.3 1.0
O B:HOH936 4.3 43.4 1.0
OH B:TYR244 4.3 20.2 1.0
O2 B:EDO509 4.3 32.7 1.0
CB B:TYR313 4.4 14.2 1.0
H11 B:EDO509 4.4 41.0 1.0
O B:HOH1030 4.5 40.5 1.0
H2 B:OD0516 4.6 18.9 1.0
C2 B:EDO509 4.6 37.7 1.0
O B:HOH787 4.7 26.6 1.0
CE2 B:TYR313 4.8 14.9 1.0
C1 B:OD0516 4.8 19.1 1.0
HG B:SER345 4.8 20.2 0.0
CD B:GLN284 4.9 17.3 1.0
CD1 B:TYR313 4.9 14.6 1.0
O B:HOH657 4.9 15.7 1.0

Reference:

S.Bhosale, S.Kandalkar, P.A.Gilormini, O.Akintola, R.J.Rowland, P.J.P.Adabala, D.King, M.C.Deen, K.Xi, G.J.Davies, D.J.Vocadlo, A.J.Bennet. Single Turnover Covalent Inhibitors For Functional Chaperoning of Lysosomal Glycoside Hydrolases To Be Published.
Page generated: Fri Jul 19 07:04:18 2024

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