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Manganese in PDB 1fbd: 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: 1fbd 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 / 2.90
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 131.600, 131.600, 68.300, 90.00, 90.00, 120.00
R / Rfree (%) 17.2 / n/a

Manganese Binding Sites:

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

Manganese binding site 1 out of 4 in 1fbd

Go back to Manganese Binding Sites List in 1fbd
Manganese 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 Manganese with other atoms in the Mn 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:Mn341

b:47.9
occ:1.00
 OE1 A:GLU280 2.4 37.2 1.0
O1P A:AHG336 2.4 58.9 1.0
OE2 A:GLU97 2.4 48.8 1.0
OD2 A:ASP118 2.4 40.9 1.0
O2P A:AHG336 2.7 51.5 1.0
CD A:GLU280 2.9 25.9 1.0
OD1 A:ASP121 2.9 13.2 1.0
P1 A:AHG336 3.0 68.2 1.0
CG A:ASP118 3.2 35.5 1.0
CD A:GLU97 3.3 45.5 1.0
OE2 A:GLU280 3.4 26.4 1.0
HH12 A:ARG276 3.4 0.0 1.0
NH1 A:ARG276 3.7 47.0 1.0
HH11 A:ARG276 3.7 0.0 1.0
MN A:MN342 3.7 51.0 1.0
CG A:GLU280 3.9 18.9 1.0
O1 A:AHG336 4.0 69.9 1.0
OD1 A:ASP118 4.0 39.2 1.0
OE1 A:GLU97 4.0 46.8 1.0
CB A:ASP118 4.1 23.9 1.0
CG A:ASP121 4.2 30.7 1.0
O3P A:AHG336 4.3 64.9 1.0
HOP3 A:AHG336 4.4 0.0 1.0
CG A:GLU97 4.4 39.1 1.0
CZ A:ARG276 4.5 49.1 1.0
CB A:ASP121 4.7 21.3 1.0
H A:GLY122 4.7 0.0 1.0
HH22 A:ARG276 4.8 0.0 1.0
CA A:ASP121 4.9 23.5 1.0
C2 A:AHG336 4.9 63.5 1.0
C1 A:AHG336 4.9 66.9 1.0
NH2 A:ARG276 5.0 50.5 1.0

Manganese binding site 2 out of 4 in 1fbd

Go back to Manganese Binding Sites List in 1fbd
Manganese 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 Manganese with other atoms in the Mn 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:Mn342

b:51.0
occ:1.00
 O A:LEU120 2.3 32.1 1.0
OD1 A:ASP118 2.4 39.2 1.0
OE1 A:GLU97 2.4 46.8 1.0
O2P A:AHG336 2.5 51.5 1.0
CG A:ASP118 3.0 35.5 1.0
OD2 A:ASP118 3.0 40.9 1.0
C A:LEU120 3.1 20.1 1.0
CD A:GLU97 3.1 45.5 1.0
H A:LEU120 3.4 0.0 1.0
CA A:ASP121 3.6 23.5 1.0
N A:ASP121 3.6 20.7 1.0
OE2 A:GLU97 3.6 48.8 1.0
HOP3 A:AHG336 3.6 0.0 1.0
P1 A:AHG336 3.6 68.2 1.0
MN A:MN341 3.7 47.9 1.0
H A:GLY122 3.7 0.0 1.0
O3P A:AHG336 3.9 64.9 1.0
N A:LEU120 4.1 16.3 1.0
OE2 A:GLU98 4.2 55.2 1.0
CA A:LEU120 4.2 16.4 1.0
O1P A:AHG336 4.3 58.9 1.0
CB A:ASP118 4.3 23.9 1.0
CB A:ASP121 4.4 21.3 1.0
CG A:GLU97 4.4 39.1 1.0
H A:ASP121 4.4 0.0 1.0
N A:GLY122 4.5 30.5 1.0
OD1 A:ASP121 4.6 13.2 1.0
C A:ASP121 4.6 28.6 1.0
OD2 A:ASP74 4.7 33.9 1.0
H A:SER123 4.7 0.0 1.0
OG A:SER123 4.7 40.6 1.0
CD A:PRO119 4.8 14.1 1.0
O1 A:AHG336 4.9 69.9 1.0
CB A:GLU97 4.9 33.1 1.0
CA A:ASP118 4.9 17.7 1.0
N A:PRO119 5.0 15.1 1.0

Manganese binding site 3 out of 4 in 1fbd

Go back to Manganese Binding Sites List in 1fbd
Manganese 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 Manganese with other atoms in the Mn 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:Mn341

b:52.4
occ:1.00
 O1P B:AHG336 2.4 66.7 1.0
OD2 B:ASP118 2.4 49.4 1.0
OE1 B:GLU280 2.4 55.9 1.0
OE1 B:GLU97 2.4 53.7 1.0
CD B:GLU280 2.9 50.7 1.0
CG B:ASP118 3.1 44.6 1.0
CD B:GLU97 3.3 52.0 1.0
P1 B:AHG336 3.3 79.8 1.0
OE2 B:GLU280 3.4 61.6 1.0
O2P B:AHG336 3.4 65.3 1.0
OD1 B:ASP121 3.6 39.9 1.0
MN B:MN342 3.6 61.7 1.0
OD1 B:ASP118 3.7 49.5 1.0
OE2 B:GLU97 3.8 55.5 1.0
CG B:GLU280 3.9 45.3 1.0
CB B:ASP118 4.1 35.7 1.0
O1 B:AHG336 4.2 75.3 1.0
CG B:GLU97 4.5 45.2 1.0
CG B:ASP121 4.5 41.4 1.0
HOP3 B:AHG336 4.5 0.0 1.0
O3P B:AHG336 4.6 78.9 1.0
CB B:ASP121 4.7 35.7 1.0
CA B:ASP121 4.8 33.2 1.0
CB B:GLU97 4.8 35.5 1.0
H B:GLY122 5.0 0.0 1.0

Manganese binding site 4 out of 4 in 1fbd

Go back to Manganese Binding Sites List in 1fbd
Manganese 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 Manganese with other atoms in the Mn 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:Mn342

b:61.7
occ:1.00
 O B:LEU120 2.4 45.9 1.0
OD1 B:ASP118 2.4 49.5 1.0
OE2 B:GLU97 2.4 55.5 1.0
O2P B:AHG336 2.4 65.3 1.0
OE2 B:GLU98 3.0 51.6 1.0
CD B:GLU97 3.1 52.0 1.0
CG B:ASP118 3.1 44.6 1.0
C B:LEU120 3.2 30.8 1.0
OD2 B:ASP118 3.2 49.4 1.0
CA B:ASP121 3.4 33.2 1.0
N B:ASP121 3.5 25.3 1.0
H B:GLY122 3.6 0.0 1.0
P1 B:AHG336 3.6 79.8 1.0
MN B:MN341 3.6 52.4 1.0
H B:LEU120 3.7 0.0 1.0
OE1 B:GLU97 3.7 53.7 1.0
O1P B:AHG336 4.0 66.7 1.0
HG B:SER123 4.0 0.0 1.0
CD B:GLU98 4.0 53.5 1.0
HOP3 B:AHG336 4.1 0.0 1.0
CG B:GLU97 4.1 45.2 1.0
H B:SER123 4.2 0.0 1.0
OG B:SER123 4.2 57.0 1.0
O3P B:AHG336 4.2 78.9 1.0
OE1 B:GLU98 4.2 53.8 1.0
N B:GLY122 4.3 38.5 1.0
N B:LEU120 4.4 26.3 1.0
H B:ASP121 4.4 0.0 1.0
C B:ASP121 4.4 37.6 1.0
CA B:LEU120 4.5 26.0 1.0
CB B:ASP121 4.5 35.7 1.0
CB B:ASP118 4.6 35.7 1.0
O1 B:AHG336 4.9 75.3 1.0
OD1 B:ASP121 4.9 39.9 1.0
CB B:GLU97 4.9 35.5 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: Tue Dec 15 03:47:55 2020

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