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Zinc in PDB 1frp: Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose-2,6-Bisphosphate, Amp and ZN2+ at 2.0 Angstroms Resolution. Aspects of Synergism Between Inhibitors

Enzymatic activity of Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose-2,6-Bisphosphate, Amp and ZN2+ at 2.0 Angstroms Resolution. Aspects of Synergism Between Inhibitors

All present enzymatic activity of Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose-2,6-Bisphosphate, Amp and ZN2+ at 2.0 Angstroms Resolution. Aspects of Synergism Between Inhibitors:
3.1.3.11;

Protein crystallography data

The structure of Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose-2,6-Bisphosphate, Amp and ZN2+ at 2.0 Angstroms Resolution. Aspects of Synergism Between Inhibitors, PDB code: 1frp was solved by Y.Xue, S.Huang, J.-Y.Liang, Y.Zhang, W.N.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 60.950, 166.300, 80.000, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose-2,6-Bisphosphate, Amp and ZN2+ at 2.0 Angstroms Resolution. Aspects of Synergism Between Inhibitors (pdb code 1frp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose-2,6-Bisphosphate, Amp and ZN2+ at 2.0 Angstroms Resolution. Aspects of Synergism Between Inhibitors, PDB code: 1frp:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1frp

Go back to Zinc Binding Sites List in 1frp
Zinc binding site 1 out of 2 in the Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose-2,6-Bisphosphate, Amp and ZN2+ at 2.0 Angstroms Resolution. Aspects of Synergism Between Inhibitors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose-2,6-Bisphosphate, Amp and ZN2+ at 2.0 Angstroms Resolution. Aspects of Synergism Between Inhibitors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn337

b:49.8
occ:1.00
 OD1 A:ASP121 2.4 24.4 1.0
OD2 A:ASP118 2.4 30.5 1.0
OE2 A:GLU280 2.4 31.2 1.0
O A:HOH339 2.5 39.4 1.0
O1 A:FDP336 2.5 36.2 1.0
H1 A:HOH339 2.6 0.0 1.0
C1 A:FDP336 3.0 20.2 1.0
CG A:ASP121 3.3 24.9 1.0
CD A:GLU280 3.3 24.8 1.0
H2 A:HOH339 3.4 0.0 1.0
HH21 A:ARG276 3.5 0.0 1.0
CG A:ASP118 3.5 24.2 1.0
CB A:ASP121 3.7 25.0 1.0
HH22 A:ARG276 3.7 0.0 1.0
H A:GLY122 3.8 0.0 1.0
O3 A:FDP336 3.8 20.7 1.0
NH2 A:ARG276 3.9 35.2 1.0
CA A:ASP121 3.9 23.9 1.0
OD1 A:ASP118 4.0 28.8 1.0
C2 A:FDP336 4.0 22.2 1.0
CG A:GLU280 4.1 22.6 1.0
OE1 A:GLU280 4.1 24.4 1.0
C3 A:FDP336 4.1 20.2 1.0
HO3 A:FDP336 4.2 0.0 1.0
H1 A:HOH446 4.3 0.0 1.0
OD2 A:ASP121 4.3 23.8 1.0
N A:GLY122 4.4 23.3 1.0
O2P A:FDP336 4.4 27.8 1.0
CB A:ASP118 4.6 20.7 1.0
O2 A:FDP336 4.6 24.1 1.0
C A:ASP121 4.8 23.4 1.0
CD1 A:ILE135 4.9 14.8 1.0
CG A:GLU97 5.0 36.1 1.0

Zinc binding site 2 out of 2 in 1frp

Go back to Zinc Binding Sites List in 1frp
Zinc binding site 2 out of 2 in the Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose-2,6-Bisphosphate, Amp and ZN2+ at 2.0 Angstroms Resolution. Aspects of Synergism Between Inhibitors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose-2,6-Bisphosphate, Amp and ZN2+ at 2.0 Angstroms Resolution. Aspects of Synergism Between Inhibitors within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn337

b:50.2
occ:1.00
 OD1 B:ASP121 2.4 27.0 1.0
OD2 B:ASP118 2.4 26.3 1.0
O B:HOH339 2.4 32.9 1.0
OE2 B:GLU280 2.5 30.6 1.0
O1 B:FDP336 2.5 35.1 1.0
H2 B:HOH339 2.7 0.0 1.0
C1 B:FDP336 2.9 23.6 1.0
CD B:GLU280 3.3 25.3 1.0
CG B:ASP121 3.4 25.8 1.0
H1 B:HOH339 3.4 0.0 1.0
CG B:ASP118 3.5 19.6 1.0
CB B:ASP121 3.7 21.7 1.0
HH21 B:ARG276 3.9 0.0 1.0
CG B:GLU280 3.9 20.1 1.0
HH22 B:ARG276 3.9 0.0 1.0
O3 B:FDP336 3.9 21.6 1.0
H B:GLY122 3.9 0.0 1.0
OD1 B:ASP118 3.9 22.1 1.0
C2 B:FDP336 4.0 23.4 1.0
CA B:ASP121 4.0 19.6 1.0
H1 B:HOH418 4.0 0.0 1.0
C3 B:FDP336 4.1 20.1 1.0
NH2 B:ARG276 4.1 35.1 1.0
OE1 B:GLU280 4.1 26.3 1.0
H2 B:HOH417 4.3 0.0 1.0
HO3 B:FDP336 4.4 0.0 1.0
OE2 B:GLU97 4.4 47.8 1.0
O B:HOH417 4.4 40.1 1.0
OD2 B:ASP121 4.4 26.2 1.0
N B:GLY122 4.5 22.4 1.0
CB B:ASP118 4.7 13.0 1.0
O2 B:FDP336 4.7 25.7 1.0
H1 B:HOH417 4.7 0.0 1.0
O2P B:FDP336 4.7 30.8 1.0
C B:ASP121 4.9 20.2 1.0
CD1 B:ILE135 4.9 17.7 1.0
O B:HOH418 4.9 52.6 1.0

Reference:

Y.Xue, S.Huang, J.Y.Liang, Y.Zhang, W.N.Lipscomb. Crystal Structure of Fructose-1,6-Bisphosphatase Complexed with Fructose 2,6-Bisphosphate, Amp, and ZN2+ at 2.0-A Resolution: Aspects of Synergism Between Inhibitors. Proc.Natl.Acad.Sci.Usa V. 91 12482 1994.
ISSN: ISSN 0027-8424
PubMed: 7809062
DOI: 10.1073/PNAS.91.26.12482
Page generated: Sun Oct 13 01:06:47 2024

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