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Zinc in PDB 1fbe: Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase

Enzymatic activity of Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase

All present enzymatic activity of Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase:
3.1.3.11;

Protein crystallography data

The structure of Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase, PDB code: 1fbe was solved by Y.Zhang, J.-Y.Liang, S.Huang, H.Ke, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 3.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 132.000, 132.000, 67.400, 90.00, 90.00, 120.00
R / Rfree (%) 19.5 / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase (pdb code 1fbe). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase, PDB code: 1fbe:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1fbe

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Zinc binding site 1 out of 4 in the Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn341

b:57.7
occ:1.00
 OE2 A:GLU280 2.3 39.9 1.0
OD2 A:ASP118 2.3 49.2 1.0
O1P A:AHG336 2.4 62.3 1.0
OE2 A:GLU97 2.5 52.1 1.0
HOP3 A:AHG336 2.6 0.0 1.0
CD A:GLU280 2.8 33.7 1.0
CG A:ASP118 2.9 40.0 1.0
OD2 A:ASP121 3.2 27.7 1.0
P1 A:AHG336 3.3 76.9 1.0
O3P A:AHG336 3.3 71.9 1.0
CG A:GLU280 3.4 25.8 1.0
OE1 A:GLU280 3.4 33.7 1.0
CD A:GLU97 3.4 55.7 1.0
OD1 A:ASP118 3.5 44.7 1.0
HH12 A:ARG276 3.6 0.0 1.0
ZN A:ZN342 3.6 67.0 1.0
CB A:ASP118 3.9 21.7 1.0
O2P A:AHG336 4.0 63.5 1.0
CG A:ASP121 4.0 22.9 1.0
NH1 A:ARG276 4.1 58.5 1.0
CG A:GLU97 4.1 47.4 1.0
OE1 A:GLU97 4.2 56.6 1.0
HH22 A:ARG276 4.3 0.0 1.0
CB A:ASP121 4.4 20.7 1.0
HH11 A:ARG276 4.4 0.0 1.0
CA A:ASP121 4.6 18.6 1.0
H A:GLY122 4.7 0.0 1.0
O1 A:AHG336 4.7 74.0 1.0
CZ A:ARG276 4.7 56.3 1.0
NH2 A:ARG276 4.8 58.3 1.0
CB A:GLU280 4.9 15.7 1.0
CD2 A:TYR279 5.0 12.4 1.0

Zinc binding site 2 out of 4 in 1fbe

Go back to Zinc Binding Sites List in 1fbe
Zinc binding site 2 out of 4 in the Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn342

b:67.0
occ:1.00
 O A:LEU120 2.4 43.1 1.0
OD1 A:ASP118 2.5 44.7 1.0
OE1 A:GLU97 2.5 56.6 1.0
O2P A:AHG336 2.6 63.5 1.0
O1P A:AHG336 3.0 62.3 1.0
CD A:GLU97 3.1 55.7 1.0
C A:LEU120 3.1 28.0 1.0
H A:GLY122 3.2 0.0 1.0
P1 A:AHG336 3.2 76.9 1.0
OE2 A:GLU97 3.2 52.1 1.0
CG A:ASP118 3.4 40.0 1.0
CA A:ASP121 3.4 18.6 1.0
ZN A:ZN341 3.6 57.7 1.0
N A:ASP121 3.7 20.5 1.0
N A:GLY122 3.9 19.4 1.0
OD2 A:ASP118 3.9 49.2 1.0
OE2 A:GLU98 4.1 72.7 1.0
H A:SER123 4.1 0.0 1.0
C A:ASP121 4.2 19.3 1.0
H A:LEU120 4.2 0.0 1.0
CB A:ASP121 4.3 20.7 1.0
O1 A:AHG336 4.4 74.0 1.0
CG A:GLU97 4.4 47.4 1.0
O3P A:AHG336 4.4 71.9 1.0
CA A:LEU120 4.5 19.8 1.0
HOP3 A:AHG336 4.6 0.0 1.0
H A:ASP121 4.6 0.0 1.0
OG A:SER123 4.7 32.2 1.0
CB A:ASP118 4.7 21.7 1.0
CB A:GLU97 4.7 41.7 1.0
N A:LEU120 4.8 17.8 1.0
HH22 A:ARG276 4.9 0.0 1.0
HG A:SER123 4.9 0.0 1.0
CG A:ASP121 4.9 22.9 1.0

Zinc binding site 3 out of 4 in 1fbe

Go back to Zinc Binding Sites List in 1fbe
Zinc binding site 3 out of 4 in the Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn341

b:72.5
occ:1.00
 OE2 B:GLU280 2.4 69.2 1.0
O1P B:AHG336 2.4 74.2 1.0
OE2 B:GLU97 2.5 72.1 1.0
OD2 B:ASP118 2.5 68.9 1.0
CD B:GLU280 3.1 64.3 1.0
CG B:ASP118 3.3 60.8 1.0
CD B:GLU97 3.3 73.5 1.0
P1 B:AHG336 3.5 78.0 1.0
OE1 B:GLU280 3.7 70.5 1.0
ZN B:ZN342 3.7 69.1 1.0
O2P B:AHG336 3.9 71.7 1.0
CG B:GLU280 3.9 60.5 1.0
OE1 B:GLU97 3.9 72.5 1.0
OD1 B:ASP118 3.9 64.3 1.0
O1 B:AHG336 4.1 72.8 1.0
OD1 B:ASP121 4.1 42.9 1.0
CB B:ASP118 4.3 49.8 1.0
CG B:GLU97 4.4 73.0 1.0
H B:GLY122 4.5 0.0 1.0
O3P B:AHG336 4.8 72.9 1.0
CB B:GLU97 4.9 70.4 1.0
CA B:ASP121 4.9 39.1 1.0
HOP3 B:AHG336 4.9 0.0 1.0

Zinc binding site 4 out of 4 in 1fbe

Go back to Zinc Binding Sites List in 1fbe
Zinc binding site 4 out of 4 in the Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn342

b:69.1
occ:1.00
 O B:LEU120 2.4 58.1 1.0
OE1 B:GLU97 2.5 72.5 1.0
OD1 B:ASP118 2.5 64.3 1.0
O2P B:AHG336 2.5 71.7 1.0
C B:LEU120 3.2 42.9 1.0
CG B:ASP118 3.2 60.8 1.0
CD B:GLU97 3.3 73.5 1.0
OD2 B:ASP118 3.3 68.9 1.0
OE2 B:GLU98 3.6 70.2 1.0
CA B:ASP121 3.6 39.1 1.0
P1 B:AHG336 3.6 78.0 1.0
H B:GLY122 3.7 0.0 1.0
N B:ASP121 3.7 37.1 1.0
ZN B:ZN341 3.7 72.5 1.0
OE1 B:GLU98 3.8 73.8 1.0
H B:SER123 3.8 0.0 1.0
O1P B:AHG336 3.8 74.2 1.0
H B:LEU120 3.9 0.0 1.0
OG B:SER123 3.9 57.7 1.0
OE2 B:GLU97 3.9 72.1 1.0
CD B:GLU98 4.1 73.3 1.0
HG B:SER123 4.2 0.0 1.0
N B:GLY122 4.2 43.0 1.0
C B:ASP121 4.2 41.1 1.0
CG B:GLU97 4.4 73.0 1.0
CA B:LEU120 4.5 38.0 1.0
N B:LEU120 4.5 37.2 1.0
H B:ASP121 4.5 0.0 1.0
HOP3 B:AHG336 4.6 0.0 1.0
O1 B:AHG336 4.7 72.8 1.0
CB B:ASP118 4.7 49.8 1.0
O3P B:AHG336 4.7 72.9 1.0
N B:SER123 4.7 51.6 1.0
CB B:GLU97 4.8 70.4 1.0
CB B:ASP121 4.9 39.4 1.0

Reference:

Y.Zhang, J.Y.Liang, S.Huang, H.Ke, W.N.Lipscomb. Crystallographic Studies of the Catalytic Mechanism of the Neutral Form of Fructose-1,6-Bisphosphatase. Biochemistry V. 32 1844 1993.
ISSN: ISSN 0006-2960
PubMed: 8382525
DOI: 10.1021/BI00058A019
Page generated: Sun Oct 13 00:53:54 2024

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