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Zinc 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:

Magnesium (Mg) 3 atoms
Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human Muscle Fructose-1,6-Bisphosphatase Q32R Mutant Complex with Amp, PDB code: 4he2:

Zinc binding site 1 out of 1 in 4he2

Go back to Zinc Binding Sites List in 4he2
Zinc binding site 1 out of 1 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 Zinc with other atoms in the Zn 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:Zn404

b:17.2
occ:0.25
 MG A:MG403 1.7 17.8 0.8
O2 A:PO3402 1.8 19.1 0.8
OE1 A:GLU97 1.9 23.7 0.5
OE2 A:GLU280 2.1 24.1 1.0
OD2 A:ASP118 2.1 25.5 1.0
P A:PO3402 2.7 25.3 0.8
OE2 A:GLU97 2.8 23.0 0.5
MG A:MG405 2.8 22.0 1.0
CD A:GLU97 2.8 24.5 0.5
CG A:ASP118 2.9 22.9 1.0
O3 A:PO3402 3.0 24.5 0.8
OE2 A:GLU97 3.1 24.7 0.5
CD A:GLU280 3.2 21.0 1.0
OD1 A:ASP118 3.2 23.1 1.0
CD A:GLU97 3.2 24.1 0.5
OE1 A:GLU97 3.4 24.6 0.5
O A:HOH740 3.5 32.3 1.0
OD1 A:ASP121 3.7 28.1 1.0
CG A:GLU280 3.9 17.8 1.0
O A:HOH625 4.0 27.4 1.0
O1 A:PO3402 4.1 19.8 0.8
O A:HOH561 4.1 24.1 1.0
OE1 A:GLU280 4.1 21.2 1.0
CG A:GLU97 4.2 23.3 0.5
CB A:ASP118 4.2 19.2 1.0
MG A:MG406 4.2 20.9 0.5
CG A:GLU97 4.3 22.8 0.5
CA A:ASP121 4.4 24.4 1.0
O A:LEU120 4.5 25.6 1.0
CG A:ASP121 4.6 26.8 1.0
O A:HOH576 4.6 25.6 1.0
CB A:ASP121 4.6 24.5 1.0
O A:HOH524 4.7 19.2 1.0
CB A:GLU97 4.8 22.9 0.5
CB A:GLU97 4.8 23.0 0.5

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: Wed Dec 16 05:22:05 2020

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