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Magnesium in PDB 4he0: Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase

Enzymatic activity of Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase

All present enzymatic activity of Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase:
3.1.3.11;

Protein crystallography data

The structure of Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase, PDB code: 4he0 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 / 2.69
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 73.853, 73.853, 146.749, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 25.3

Other elements in 4he0:

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

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase (pdb code 4he0). 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, PDB code: 4he0:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 4he0

Go back to Magnesium Binding Sites List in 4he0
Magnesium binding site 1 out of 3 in the Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:35.5
occ:1.00
OD2 A:ASP118 2.0 29.3 1.0
O1 A:PO4401 2.1 58.3 1.0
OE2 A:GLU280 2.2 28.1 1.0
O3 A:PO4401 2.3 56.2 1.0
OD1 A:ASP121 2.3 33.6 1.0
P A:PO4401 2.7 56.9 1.0
MG A:MG403 3.0 33.2 1.0
NH1 A:ARG276 3.1 40.7 1.0
OE2 A:GLU97 3.1 34.8 1.0
CG A:ASP118 3.1 28.2 1.0
CD A:GLU280 3.3 25.4 1.0
CG A:ASP121 3.4 34.5 1.0
O2 A:PO4401 3.4 56.5 1.0
OD1 A:ASP118 3.5 29.8 1.0
CG A:GLU280 3.8 21.6 1.0
CB A:ASP121 3.8 33.4 1.0
CA A:ASP121 3.9 33.7 1.0
O4 A:PO4401 4.0 56.2 1.0
CD A:GLU97 4.1 35.4 1.0
OE1 A:GLU280 4.3 25.6 1.0
CZ A:ARG276 4.3 41.2 1.0
CB A:ASP118 4.4 25.7 1.0
OD2 A:ASP121 4.5 35.1 1.0
O A:LEU120 4.6 33.2 1.0
OE1 A:GLU97 4.7 38.5 1.0
N A:GLY122 4.7 36.5 1.0
N A:ASP121 4.9 32.2 1.0
C A:ASP121 4.9 34.9 1.0
NE A:ARG276 5.0 39.8 1.0

Magnesium binding site 2 out of 3 in 4he0

Go back to Magnesium Binding Sites List in 4he0
Magnesium binding site 2 out of 3 in the Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg403

b:33.2
occ:1.00
O1 A:PO4401 1.9 58.3 1.0
OE2 A:GLU97 2.0 34.8 1.0
OD1 A:ASP118 2.1 29.8 1.0
O A:LEU120 2.5 33.2 1.0
O A:HOH547 2.6 30.5 1.0
CG A:ASP118 3.0 28.2 1.0
MG A:MG402 3.0 35.5 1.0
CD A:GLU97 3.1 35.4 1.0
OD2 A:ASP118 3.1 29.3 1.0
P A:PO4401 3.2 56.9 1.0
O2 A:PO4401 3.3 56.5 1.0
C A:LEU120 3.4 31.7 1.0
OE1 A:GLU97 3.6 38.5 1.0
MG A:MG404 3.8 56.7 1.0
CA A:ASP121 3.9 33.7 1.0
OE2 A:GLU98 3.9 37.1 1.0
N A:ASP121 4.0 32.2 1.0
O4 A:PO4401 4.1 56.2 1.0
O3 A:PO4401 4.1 56.2 1.0
CG A:GLU97 4.3 33.7 1.0
N A:LEU120 4.3 29.2 1.0
OG A:SER123 4.3 43.6 1.0
CB A:ASP118 4.4 25.7 1.0
CA A:LEU120 4.4 30.7 1.0
CB A:GLU97 4.4 30.8 1.0
OD1 A:ASP121 4.5 33.6 1.0
NH1 A:ARG276 4.5 40.7 1.0
OD1 A:ASP74 4.6 45.6 1.0
CB A:ASP121 4.6 33.4 1.0
CD A:PRO119 4.8 27.6 1.0
CA A:ASP118 4.8 25.5 1.0
C A:ASP118 4.9 26.0 1.0
OE2 A:GLU280 4.9 28.1 1.0
C A:ASP121 5.0 34.9 1.0

Magnesium binding site 3 out of 3 in 4he0

Go back to Magnesium Binding Sites List in 4he0
Magnesium binding site 3 out of 3 in the Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg404

b:56.7
occ:1.00
O2 A:PO4401 2.2 56.5 1.0
OE1 A:GLU97 2.7 38.5 1.0
OD2 A:ASP68 3.2 69.0 1.0
CB A:ASP68 3.4 69.2 1.0
P A:PO4401 3.4 56.9 1.0
O A:HOH548 3.6 28.1 1.0
CD A:GLU97 3.6 35.4 1.0
ND2 A:ASN64 3.7 69.5 1.0
O4 A:PO4401 3.8 56.2 1.0
OE2 A:GLU98 3.8 37.1 1.0
CG A:ASP68 3.8 69.2 1.0
MG A:MG403 3.8 33.2 1.0
OG A:SER123 3.8 43.6 1.0
OE2 A:GLU97 3.9 34.8 1.0
OD2 A:ASP74 3.9 47.1 1.0
O1 A:PO4401 3.9 58.3 1.0
CB A:SER123 4.4 44.8 1.0
O A:HOH547 4.6 30.5 1.0
CG A:ASP74 4.6 44.8 1.0
OD1 A:ASP74 4.6 45.6 1.0
O3 A:PO4401 4.7 56.2 1.0
CD A:GLU98 4.8 36.1 1.0
NH1 A:ARG276 4.8 40.7 1.0
CG A:ASN64 4.8 70.9 1.0
CA A:ASP68 4.8 70.8 1.0
NH2 A:ARG276 4.9 39.7 1.0
OE1 A:GLU98 4.9 39.8 1.0
OD1 A:ASP68 5.0 70.6 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 16:16:24 2024

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