Atomistry » Magnesium » PDB 4kvy-4la6 » 4kxp
Atomistry »
  Magnesium »
    PDB 4kvy-4la6 »
      4kxp »

Magnesium in PDB 4kxp: Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State

Enzymatic activity of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State

All present enzymatic activity of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State:
3.1.3.11;

Protein crystallography data

The structure of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State, PDB code: 4kxp was solved by C.V.Iancu, S.Mukund, J.-Y.Choe, H.J.Fromm, R.B.Honzatko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.66 / 2.70
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 59.544, 166.382, 78.946, 90.00, 90.00, 90.00
R / Rfree (%) 20.4 / 25.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State (pdb code 4kxp). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State, PDB code: 4kxp:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 4kxp

Go back to Magnesium Binding Sites List in 4kxp
Magnesium binding site 1 out of 4 in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:2.0
occ:1.00
 OD2 A:ASP121 1.8 19.1 1.0
OD2 A:ASP118 1.8 19.9 1.0
OE2 A:GLU280 1.8 23.3 1.0
O2 A:PO4402 1.9 30.2 1.0
CG A:ASP121 2.8 22.0 1.0
CG A:ASP118 2.9 22.4 1.0
CD A:GLU280 3.0 21.4 1.0
O1 A:PO4402 3.0 27.6 1.0
P A:PO4402 3.0 29.7 1.0
CB A:ASP121 3.3 21.2 1.0
OD1 A:ASP118 3.3 23.7 1.0
CG A:GLU280 3.5 23.6 1.0
CA A:ASP121 3.6 21.4 1.0
O3 A:PO4402 3.7 22.5 1.0
NH2 A:ARG276 3.8 37.8 1.0
OD1 A:ASP121 3.9 24.2 1.0
OE1 A:GLU280 4.0 22.8 1.0
O3 A:F6P401 4.1 12.6 1.0
CB A:ASP118 4.2 22.0 1.0
O4 A:PO4402 4.2 29.8 1.0
OE2 A:GLU97 4.3 21.4 1.0
C1 A:F6P401 4.5 17.5 1.0
N A:GLY122 4.5 21.4 1.0
MG A:MG404 4.6 61.4 1.0
C A:ASP121 4.6 21.5 1.0
O1 A:F6P401 4.6 19.3 1.0
N A:ASP121 4.7 20.3 1.0
CD1 A:ILE135 4.7 17.8 1.0
C3 A:F6P401 4.9 15.8 1.0
CZ A:ARG276 4.9 37.4 1.0
O A:LEU120 4.9 20.0 1.0
CE A:MET248 4.9 16.1 1.0
CB A:GLU280 5.0 23.9 1.0
CD A:GLU97 5.0 23.8 1.0

Magnesium binding site 2 out of 4 in 4kxp

Go back to Magnesium Binding Sites List in 4kxp
Magnesium binding site 2 out of 4 in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg404

b:61.4
occ:1.00
 OD1 A:ASP118 2.3 23.7 1.0
OE2 A:GLU97 2.4 21.4 1.0
O A:LEU120 2.6 20.0 1.0
O1 A:PO4402 2.7 27.6 1.0
C A:LEU120 3.2 19.8 1.0
N A:LEU120 3.2 19.9 1.0
CG A:ASP118 3.4 22.4 1.0
CD A:PRO119 3.5 20.7 1.0
CD A:GLU97 3.6 23.8 1.0
CA A:LEU120 3.8 20.1 1.0
N A:PRO119 3.9 21.8 1.0
C A:ASP118 3.9 21.7 1.0
N A:ASP121 4.0 20.3 1.0
OE2 A:GLU98 4.0 35.5 1.0
OD2 A:ASP118 4.1 19.9 1.0
P A:PO4402 4.2 29.7 1.0
C A:PRO119 4.3 19.8 1.0
CA A:ASP121 4.3 21.4 1.0
O A:ASP118 4.3 20.5 1.0
CA A:ASP118 4.3 21.7 1.0
CB A:LEU120 4.4 20.1 1.0
CB A:GLU97 4.4 25.0 1.0
CG A:PRO119 4.4 21.1 1.0
CA A:PRO119 4.5 20.6 1.0
CB A:ASP118 4.5 22.0 1.0
OE1 A:GLU97 4.5 24.9 1.0
CB A:PRO119 4.5 20.1 1.0
CG A:GLU97 4.5 23.8 1.0
MG A:MG403 4.6 2.0 1.0
OD1 A:ASP74 4.6 49.8 1.0
CG A:GLU98 4.8 31.8 1.0
O2 A:PO4402 4.8 30.2 1.0
O4 A:PO4402 4.8 29.8 1.0
CD A:GLU98 4.8 34.3 1.0
O A:HOH512 4.9 35.7 1.0
O3 A:PO4402 5.0 22.5 1.0

Magnesium binding site 3 out of 4 in 4kxp

Go back to Magnesium Binding Sites List in 4kxp
Magnesium binding site 3 out of 4 in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg403

b:2.0
occ:1.00
 OD2 B:ASP118 1.8 23.5 1.0
OD2 B:ASP121 1.9 9.6 1.0
O3 B:PO4402 1.9 29.3 1.0
OE1 B:GLU280 2.0 23.1 1.0
CG B:ASP121 2.6 16.5 1.0
CG B:ASP118 2.8 19.8 1.0
P B:PO4402 3.1 28.6 1.0
CB B:ASP121 3.1 15.2 1.0
CD B:GLU280 3.1 21.9 1.0
OD1 B:ASP118 3.2 24.4 1.0
O4 B:PO4402 3.4 28.0 1.0
CA B:ASP121 3.5 16.0 1.0
OD1 B:ASP121 3.6 17.6 1.0
CG B:GLU280 3.6 18.8 1.0
O2 B:PO4402 3.7 27.5 1.0
CB B:ASP118 4.2 17.6 1.0
OE2 B:GLU280 4.2 22.1 1.0
OE1 B:GLU97 4.3 36.1 1.0
O1 B:PO4402 4.3 33.3 1.0
O3 B:F6P401 4.4 16.4 1.0
C1 B:F6P401 4.4 17.9 1.0
N B:ASP121 4.5 15.8 1.0
N B:GLY122 4.5 17.9 1.0
C B:ASP121 4.5 16.9 1.0
NH1 B:ARG276 4.5 31.0 1.0
O1 B:F6P401 4.6 16.7 1.0
O B:LEU120 4.6 17.6 1.0
O2 B:F6P401 4.8 17.1 1.0
C B:LEU120 4.9 16.8 1.0
C3 B:F6P401 5.0 16.7 1.0
CD B:GLU97 5.0 33.7 1.0
C2 B:F6P401 5.0 16.6 1.0

Magnesium binding site 4 out of 4 in 4kxp

Go back to Magnesium Binding Sites List in 4kxp
Magnesium binding site 4 out of 4 in the Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Amp Complexes of Porcine Liver Fructose-1,6- Bisphosphatase Mutant I10D in T-State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg404

b:35.5
occ:1.00
 OD2 B:ASP74 2.6 46.8 1.0
O B:LEU120 2.8 17.6 1.0
OE1 B:GLU97 3.1 36.1 1.0
N B:LEU120 3.1 16.6 1.0
OD1 B:ASP118 3.2 24.4 1.0
CG B:PRO119 3.3 18.5 1.0
O4 B:PO4402 3.4 28.0 1.0
OE1 B:GLU98 3.5 30.3 1.0
C B:LEU120 3.5 16.8 1.0
CD B:PRO119 3.7 17.6 1.0
CA B:LEU120 3.7 17.0 1.0
CG B:ASP74 3.7 43.0 1.0
O B:HOH547 4.0 39.4 1.0
CB B:LEU120 4.0 17.8 1.0
N B:PRO119 4.0 17.0 1.0
CD B:GLU98 4.1 29.5 1.0
CG B:GLU98 4.1 30.4 1.0
C B:PRO119 4.2 17.0 1.0
OD1 B:ASP74 4.2 42.4 1.0
CD B:GLU97 4.2 33.7 1.0
CB B:PRO119 4.2 17.1 1.0
CA B:PRO119 4.4 17.1 1.0
CG B:ASP118 4.4 19.8 1.0
N B:ASP121 4.5 15.8 1.0
C B:ASP118 4.5 18.1 1.0
P B:PO4402 4.8 28.6 1.0
CB B:GLU97 4.9 28.9 1.0
CB B:ASP74 4.9 40.6 1.0
OE2 B:GLU97 4.9 34.4 1.0
CA B:ASP118 4.9 17.6 1.0

Reference:

Y.Gao, C.V.Iancu, S.Mukind, J.Y.Choe, R.B.Honzatko. Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Mammalian Fructose-1,6-Bisphosphatase. Biochemistry V. 52 5206 2013.
ISSN: ISSN 0006-2960
PubMed: 23844654
DOI: 10.1021/BI400532N
Page generated: Sat Aug 17 04:23:53 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy