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Chlorine in PDB 1lev: Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor

Enzymatic activity of Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor

All present enzymatic activity of Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor:
3.1.3.11;

Protein crystallography data

The structure of Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor, PDB code: 1lev was solved by S.W.Wright, A.A.Carlo, D.E.Danley, D.L.Hageman, G.A.Karam, M.N.Mansour, L.D.Mcclure, J.Pandit, G.K.Schulte, J.L.Treadway, I.-K.Wang, P.H.Bauer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.26 / 2.15
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 118.870, 73.446, 78.025, 90.00, 106.30, 90.00
R / Rfree (%) 19.3 / 25.5

Other elements in 1lev:

The structure of Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor also contains other interesting chemical elements:

Manganese (Mn) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor (pdb code 1lev). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor, PDB code: 1lev:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 1lev

Go back to Chlorine Binding Sites List in 1lev
Chlorine binding site 1 out of 4 in the Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl342

b:36.8
occ:1.00
 CL17 A:CLI342 0.0 36.8 1.0
C13 A:CLI342 1.7 43.3 1.0
C8 A:CLI342 2.7 40.9 1.0
C9 A:CLI342 2.7 44.2 1.0
CG1 A:VAL17 3.7 31.5 1.0
CD1 A:LEU34 3.7 24.3 1.0
CB A:VAL17 3.7 37.9 1.0
CD2 A:LEU175 3.8 17.2 1.0
CB A:GLU20 3.8 49.9 1.0
CA A:VAL17 3.8 39.2 1.0
CE1 A:PHE16 3.9 27.3 1.0
C3 A:CLI342 4.0 46.2 1.0
C4 A:CLI342 4.0 47.9 1.0
CG A:GLU20 4.0 47.0 1.0
CG A:MET177 4.2 36.7 1.0
CD1 A:PHE16 4.3 26.0 1.0
SD A:MET177 4.3 45.9 1.0
C1 A:CLI342 4.5 46.8 1.0
O A:VAL17 4.6 42.1 1.0
CG A:LEU175 4.7 21.1 1.0
C A:VAL17 4.7 41.5 1.0
N A:VAL17 4.8 35.6 1.0
CZ A:PHE16 4.9 25.3 1.0

Chlorine binding site 2 out of 4 in 1lev

Go back to Chlorine Binding Sites List in 1lev
Chlorine binding site 2 out of 4 in the Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl342

b:57.4
occ:1.00
 CL10 A:CLI342 0.0 57.4 1.0
C4 A:CLI342 1.7 47.9 1.0
C1 A:CLI342 2.7 46.8 1.0
C9 A:CLI342 2.7 44.2 1.0
C6 A:CLI342 3.1 51.7 1.0
C2 A:CLI342 3.3 48.7 1.0
O A:HOH389 3.6 30.4 1.0
C3 A:CLI342 4.0 46.2 1.0
C13 A:CLI342 4.0 43.3 1.0
CG1 A:VAL160 4.4 23.4 1.0
C5 A:CLI342 4.5 50.1 1.0
C8 A:CLI342 4.6 40.9 1.0
C12 A:CLI342 4.6 58.7 1.0
CB A:ALA24 4.7 67.2 1.0
O A:HOH388 4.8 39.1 1.0
O A:VAL160 4.8 20.8 1.0
CB A:MET177 4.9 31.2 1.0
N7 A:CLI342 4.9 50.4 1.0
CG A:MET30 5.0 31.9 1.0

Chlorine binding site 3 out of 4 in 1lev

Go back to Chlorine Binding Sites List in 1lev
Chlorine binding site 3 out of 4 in the Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cl339

b:83.4
occ:1.00
 CL17 F:CLI339 0.0 83.4 1.0
C13 F:CLI339 1.7 82.5 1.0
C9 F:CLI339 2.6 83.1 1.0
C8 F:CLI339 2.7 82.6 1.0
CG1 F:VAL17 3.3 29.9 1.0
CA F:VAL17 3.3 39.7 1.0
CB F:VAL17 3.4 38.6 1.0
CE1 F:PHE16 3.5 29.1 1.0
CD1 F:PHE16 3.8 29.6 1.0
CB F:GLU20 3.8 51.2 1.0
CG F:GLU20 3.9 49.5 1.0
C4 F:CLI339 3.9 84.2 1.0
CD2 F:LEU175 3.9 20.1 1.0
C3 F:CLI339 4.0 82.3 1.0
O F:VAL17 4.2 43.7 1.0
C F:VAL17 4.3 42.2 1.0
CD1 F:LEU34 4.3 27.0 1.0
N F:VAL17 4.3 37.1 1.0
C1 F:CLI339 4.5 84.1 1.0
O F:PHE16 4.5 33.0 1.0
CE F:MET177 4.6 47.3 1.0
CZ F:PHE16 4.6 29.4 1.0
C F:PHE16 4.7 34.6 1.0
CG2 F:VAL17 4.9 38.7 1.0

Chlorine binding site 4 out of 4 in 1lev

Go back to Chlorine Binding Sites List in 1lev
Chlorine binding site 4 out of 4 in the Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Porcine Kidney Fructose-1,6-Bisphosphatase Complexed with An Amp-Site Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cl339

b:90.3
occ:1.00
 CL10 F:CLI339 0.0 90.3 1.0
C4 F:CLI339 1.7 84.2 1.0
C9 F:CLI339 2.6 83.1 1.0
C1 F:CLI339 2.7 84.1 1.0
O F:VAL160 3.1 21.9 1.0
C6 F:CLI339 3.2 84.5 1.0
C2 F:CLI339 3.3 83.8 1.0
O F:HOH349 3.4 28.4 1.0
CG1 F:VAL160 3.5 28.2 1.0
CB F:MET177 3.5 30.2 1.0
C13 F:CLI339 3.9 82.5 1.0
CE F:MET177 3.9 47.3 1.0
C3 F:CLI339 4.0 82.3 1.0
CB F:ALA161 4.1 18.3 1.0
C F:VAL160 4.1 23.4 1.0
CG F:MET177 4.4 41.9 1.0
C8 F:CLI339 4.5 82.6 1.0
C12 F:CLI339 4.5 83.1 1.0
C5 F:CLI339 4.6 82.4 1.0
CA F:MET177 4.7 30.0 1.0
CE F:MET30 4.7 29.4 1.0
CB F:VAL160 4.8 24.3 1.0
CA F:ALA161 4.8 23.7 1.0
CG F:MET30 4.8 34.7 1.0
N F:ALA161 4.9 21.5 1.0
N7 F:CLI339 4.9 82.6 1.0
CA F:VAL160 4.9 23.6 1.0
SD F:MET177 5.0 57.1 1.0

Reference:

S.W.Wright, A.A.Carlo, D.E.Danley, D.L.Hageman, G.A.Karam, M.N.Mansour, L.D.Mcclure, J.Pandit, G.K.Schulte, J.L.Treadway, I.-K.Wang, P.H.Bauer. 3-(2-Carboxyethyl)-4,6-Dichloro-1H-Indole-2-Carboxylic Acid: An Allosteric Inhibitor of Fructose-1,6-Bisphosphatase at the Amp Site. Bioorg.Med.Chem.Lett. V. 13 2055 2003.
ISSN: ISSN 0960-894X
PubMed: 12781194
DOI: 10.1016/S0960-894X(03)00310-X
Page generated: Thu Jul 10 18:01:34 2025

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