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Zinc in PDB 1eyk: Fructose-1,6-Bisphosphatase Complex with Amp, Zinc, Fructose-6- Phosphate and Phosphate (T-State)

Enzymatic activity of Fructose-1,6-Bisphosphatase Complex with Amp, Zinc, Fructose-6- Phosphate and Phosphate (T-State)

All present enzymatic activity of Fructose-1,6-Bisphosphatase Complex with Amp, Zinc, Fructose-6- Phosphate and Phosphate (T-State):
3.1.3.11;

Protein crystallography data

The structure of Fructose-1,6-Bisphosphatase Complex with Amp, Zinc, Fructose-6- Phosphate and Phosphate (T-State), PDB code: 1eyk was solved by J.Choe, R.B.Honzatko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 2.23
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 60.120, 166.140, 79.530, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 27.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Fructose-1,6-Bisphosphatase Complex with Amp, Zinc, Fructose-6- Phosphate and Phosphate (T-State) (pdb code 1eyk). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Fructose-1,6-Bisphosphatase Complex with Amp, Zinc, Fructose-6- Phosphate and Phosphate (T-State), PDB code: 1eyk:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1eyk

Go back to Zinc Binding Sites List in 1eyk
Zinc binding site 1 out of 2 in the Fructose-1,6-Bisphosphatase Complex with Amp, Zinc, Fructose-6- Phosphate and Phosphate (T-State)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Fructose-1,6-Bisphosphatase Complex with Amp, Zinc, Fructose-6- Phosphate and Phosphate (T-State) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn339

b:18.5
occ:1.00
OD2 A:ASP118 1.9 16.7 1.0
O4 A:PO4340 2.1 30.0 1.0
OD2 A:ASP121 2.2 14.7 1.0
OE2 A:GLU280 2.3 18.9 1.0
CG A:ASP118 2.9 17.1 1.0
OD1 A:ASP118 3.2 16.3 1.0
CG A:ASP121 3.2 16.7 1.0
CD A:GLU280 3.3 20.2 1.0
P A:PO4340 3.3 30.4 1.0
O1 A:PO4340 3.3 29.6 1.0
CB A:ASP121 3.6 16.7 1.0
CG A:GLU280 3.7 20.1 1.0
CA A:ASP121 3.7 17.4 1.0
NH2 A:ARG276 4.0 27.6 1.0
C1 A:F6P338 4.1 17.7 1.0
O2 A:PO4340 4.2 29.8 1.0
CB A:ASP118 4.2 17.0 1.0
O3 A:PO4340 4.3 29.6 1.0
OD1 A:ASP121 4.3 17.3 1.0
O3 A:F6P338 4.4 14.3 1.0
OE1 A:GLU280 4.4 21.0 1.0
O A:HOH502 4.4 27.1 1.0
CD1 A:ILE135 4.5 14.8 1.0
N A:GLY122 4.5 18.5 1.0
N A:ASP121 4.6 18.0 1.0
C A:ASP121 4.6 17.8 1.0
O1 A:F6P338 4.7 21.0 1.0
C2 A:F6P338 4.8 17.2 1.0
CE A:MET248 4.8 17.9 1.0
CG A:GLU97 4.8 24.9 1.0
C3 A:F6P338 4.9 15.9 1.0
O2 A:F6P338 4.9 15.8 1.0
OE1 A:GLU97 4.9 25.6 1.0
O A:LEU120 5.0 18.8 1.0

Zinc binding site 2 out of 2 in 1eyk

Go back to Zinc Binding Sites List in 1eyk
Zinc binding site 2 out of 2 in the Fructose-1,6-Bisphosphatase Complex with Amp, Zinc, Fructose-6- Phosphate and Phosphate (T-State)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Fructose-1,6-Bisphosphatase Complex with Amp, Zinc, Fructose-6- Phosphate and Phosphate (T-State) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn344

b:18.1
occ:1.00
OD2 B:ASP121 2.0 11.7 1.0
O1 B:PO4343 2.0 26.9 1.0
OD2 B:ASP118 2.0 15.6 1.0
OE1 B:GLU280 2.1 18.1 1.0
CG B:ASP121 3.0 13.6 1.0
CG B:ASP118 3.0 16.5 1.0
CD B:GLU280 3.2 19.2 1.0
P B:PO4343 3.2 26.9 1.0
O4 B:PO4343 3.3 27.0 1.0
OD1 B:ASP118 3.3 15.5 1.0
CB B:ASP121 3.4 14.1 1.0
CG B:GLU280 3.6 19.0 1.0
CA B:ASP121 3.7 15.8 1.0
NH2 B:ARG276 3.9 20.4 1.0
C1 B:F6P341 4.0 24.8 1.0
O3 B:PO4343 4.0 26.7 1.0
OD1 B:ASP121 4.1 14.4 1.0
O2 B:PO4343 4.3 26.5 1.0
OE2 B:GLU280 4.3 19.8 1.0
CB B:ASP118 4.4 16.7 1.0
O3 B:F6P341 4.4 24.0 1.0
N B:GLY122 4.5 16.7 1.0
O B:HOH501 4.6 26.7 1.0
N B:ASP121 4.6 16.1 1.0
C B:ASP121 4.6 16.4 1.0
C2 B:F6P341 4.8 24.4 1.0
C3 B:F6P341 4.9 23.9 1.0
O1 B:F6P341 4.9 25.2 1.0
CZ B:ARG276 5.0 21.7 1.0
O2 B:F6P341 5.0 24.6 1.0
OE1 B:GLU97 5.0 22.8 1.0
CG B:GLU97 5.0 21.6 1.0

Reference:

J.Y.Choe, H.J.Fromm, R.B.Honzatko. Crystal Structures of Fructose 1,6-Bisphosphatase: Mechanism of Catalysis and Allosteric Inhibition Revealed in Product Complexes. Biochemistry V. 39 8565 2000.
ISSN: ISSN 0006-2960
PubMed: 10913263
DOI: 10.1021/BI000574G
Page generated: Sun Oct 13 00:34:32 2024

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