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Magnesium in PDB 4he2: Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp

Enzymatic activity of Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp

All present enzymatic activity of Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp:
3.1.3.11;

Protein crystallography data

The structure of Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp, PDB code: 4he2 was solved by R.Shi, D.W.Zhu, S.X.Lin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.60
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 73.366, 73.366, 146.622, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 19.4

Other elements in 4he2:

The structure of Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Zinc (Zn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp (pdb code 4he2). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp, PDB code: 4he2:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 4he2

Go back to Magnesium Binding Sites List in 4he2
Magnesium binding site 1 out of 3 in the Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp


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 Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:17.8
occ:0.75
 ZN A:ZN404 1.7 17.2 0.2
OD1 A:ASP121 1.9 28.1 1.0
O2 A:PO3402 2.1 19.1 0.8
OE2 A:GLU280 2.2 24.1 1.0
OD2 A:ASP118 2.3 25.5 1.0
O A:HOH740 2.5 32.3 1.0
P A:PO3402 2.8 25.3 0.8
CG A:ASP121 3.0 26.8 1.0
CD A:GLU280 3.3 21.0 1.0
CB A:ASP121 3.4 24.5 1.0
CG A:ASP118 3.4 22.9 1.0
CA A:ASP121 3.5 24.4 1.0
O3 A:PO3402 3.6 24.5 0.8
OE1 A:GLU97 3.7 23.7 0.5
MG A:MG405 3.7 22.0 1.0
O1 A:PO3402 3.8 19.8 0.8
CG A:GLU280 3.8 17.8 1.0
OD1 A:ASP118 3.9 23.1 1.0
OD2 A:ASP121 4.1 28.4 1.0
O A:HOH741 4.1 16.4 1.0
N A:GLY122 4.2 26.0 1.0
OE1 A:GLU280 4.3 21.2 1.0
O A:HOH625 4.3 27.4 1.0
C A:ASP121 4.4 25.3 1.0
OE2 A:GLU97 4.4 23.0 0.5
CE A:MET248 4.4 14.0 0.5
CD A:GLU97 4.6 24.5 0.5
CB A:ASP118 4.6 19.2 1.0
N A:ASP121 4.6 23.3 1.0
OE2 A:GLU97 4.6 24.7 0.5
CD1 A:ILE135 4.7 20.9 1.0
O A:LEU120 4.7 25.6 1.0
O A:HOH561 4.8 24.1 1.0
CD A:GLU97 4.9 24.1 0.5

Magnesium binding site 2 out of 3 in 4he2

Go back to Magnesium Binding Sites List in 4he2
Magnesium binding site 2 out of 3 in the Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp


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 Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg405

b:22.0
occ:1.00
 O2 A:PO3402 1.9 19.1 0.8
O A:HOH524 2.0 19.2 1.0
OE2 A:GLU97 2.1 23.0 0.5
O A:HOH561 2.1 24.1 1.0
OE2 A:GLU97 2.1 24.7 0.5
OD1 A:ASP118 2.2 23.1 1.0
O A:LEU120 2.2 25.6 1.0
ZN A:ZN404 2.8 17.2 0.2
CD A:GLU97 3.0 24.5 0.5
P A:PO3402 3.0 25.3 0.8
CG A:ASP118 3.0 22.9 1.0
CD A:GLU97 3.1 24.1 0.5
C A:LEU120 3.2 23.2 1.0
OD2 A:ASP118 3.2 25.5 1.0
OE1 A:GLU97 3.3 23.7 0.5
OE1 A:GLU97 3.6 24.6 0.5
O3 A:PO3402 3.7 24.5 0.8
MG A:MG403 3.7 17.8 0.8
MG A:MG406 3.7 20.9 0.5
CA A:ASP121 3.8 24.4 1.0
N A:ASP121 3.9 23.3 1.0
O1 A:PO3402 3.9 19.8 0.8
OE2 A:GLU98 4.0 33.2 1.0
OD1 A:ASP74 4.0 42.7 1.0
O A:HOH600 4.2 27.7 1.0
N A:LEU120 4.2 21.6 1.0
CA A:LEU120 4.3 22.8 0.5
CA A:LEU120 4.3 23.0 0.5
CG A:GLU97 4.3 23.3 0.5
OG A:SER123 4.3 35.6 1.0
CG A:GLU97 4.4 22.8 0.5
CB A:ASP118 4.4 19.2 1.0
CB A:GLU97 4.6 23.0 0.5
CB A:GLU97 4.6 22.9 0.5
CB A:ASP121 4.8 24.5 1.0
CD A:PRO119 4.8 20.6 1.0
C A:ASP121 4.9 25.3 1.0
CA A:ASP118 4.9 19.3 1.0
OE2 A:GLU280 4.9 24.1 1.0
CB A:LEU120 4.9 23.8 0.5
O A:HOH628 4.9 20.0 1.0
C A:ASP118 4.9 19.5 1.0
N A:PRO119 4.9 19.8 1.0
N A:GLY122 5.0 26.0 1.0
CB A:LEU120 5.0 24.0 0.5
OD1 A:ASP121 5.0 28.1 1.0

Magnesium binding site 3 out of 3 in 4he2

Go back to Magnesium Binding Sites List in 4he2
Magnesium binding site 3 out of 3 in the Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp


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 Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg406

b:20.9
occ:0.50
 O A:HOH628 1.9 20.0 1.0
O3 A:PO3402 2.0 24.5 0.8
O A:HOH600 2.1 27.7 1.0
O A:HOH757 2.2 31.6 1.0
OE1 A:GLU97 2.3 24.6 0.5
O A:HOH561 2.4 24.1 1.0
P A:PO3402 2.9 25.3 0.8
OE2 A:GLU97 3.0 24.7 0.5
CD A:GLU97 3.3 24.1 0.5
O1 A:PO3402 3.6 19.8 0.8
OE2 A:GLU97 3.6 23.0 0.5
CD A:GLU97 3.6 24.5 0.5
O2 A:PO3402 3.6 19.1 0.8
MG A:MG405 3.7 22.0 1.0
O A:HOH649 3.7 36.7 1.0
OE1 A:GLU97 3.9 23.7 0.5
OG A:SER123 4.2 35.6 1.0
ZN A:ZN404 4.2 17.2 0.2
OE2 A:GLU98 4.2 33.2 1.0
O A:HOH576 4.3 25.6 1.0
O A:HOH524 4.5 19.2 1.0
O A:HOH648 4.6 39.4 1.0
CG A:GLU97 4.6 22.8 0.5
CG A:GLU97 4.6 23.3 0.5
CB A:SER123 4.7 34.1 1.0
OD1 A:ASP74 4.8 42.7 1.0

Reference:

R.Shi, Z.Y.Chen, D.W.Zhu, C.Li, Y.Shan, G.Xu, S.X.Lin. Crystal Structures of Human Muscle Fructose-1,6-Bisphosphatase: Novel Quaternary States, Enhanced Amp Affinity, and Allosteric Signal Transmission Pathway. Plos One V. 8 71242 2013.
ISSN: ESSN 1932-6203
PubMed: 24086250
DOI: 10.1371/JOURNAL.PONE.0071242
Page generated: Fri Aug 16 16:16:41 2024

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