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Zinc in PDB 1e48: L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant E73Q/Y113F/Y209F

Enzymatic activity of L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant E73Q/Y113F/Y209F

All present enzymatic activity of L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant E73Q/Y113F/Y209F:
4.1.2.17;

Protein crystallography data

The structure of L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant E73Q/Y113F/Y209F, PDB code: 1e48 was solved by A.C.Joerger, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.97
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 93.700, 93.700, 43.200, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 22.1

Zinc Binding Sites:

The binding sites of Zinc atom in the L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant E73Q/Y113F/Y209F (pdb code 1e48). 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 L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant E73Q/Y113F/Y209F, PDB code: 1e48:

Zinc binding site 1 out of 1 in 1e48

Go back to Zinc Binding Sites List in 1e48
Zinc binding site 1 out of 1 in the L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant E73Q/Y113F/Y209F


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant E73Q/Y113F/Y209F within 5.0Å range:
probe atom residue distance (Å) B Occ
P:Zn303

b:17.2
occ:1.00
O3 P:13P302 1.7 21.6 0.7
NE2 P:HIS92 2.1 11.1 1.0
NE2 P:HIS94 2.1 12.7 1.0
NE2 P:HIS155 2.1 7.7 1.0
O2 P:13P302 2.6 24.9 0.7
C3 P:13P302 2.8 25.6 0.7
NE2 P:GLN73 3.0 35.4 0.7
CE1 P:HIS92 3.0 11.0 1.0
CD2 P:HIS94 3.0 11.5 1.0
CD2 P:HIS155 3.1 10.4 1.0
CD2 P:HIS92 3.1 10.9 1.0
CE1 P:HIS94 3.1 12.4 1.0
C2 P:13P302 3.2 26.6 0.7
CE1 P:HIS155 3.2 9.5 1.0
ND1 P:HIS92 4.1 11.7 1.0
CD P:GLN73 4.2 34.2 0.7
CG P:HIS92 4.2 12.8 1.0
CG P:HIS94 4.2 12.0 1.0
ND1 P:HIS94 4.2 11.6 1.0
ND1 P:HIS155 4.2 10.9 1.0
CG P:HIS155 4.3 8.7 1.0
CG P:GLN73 4.5 26.9 0.3
O P:ALA27 4.5 44.5 1.0
CG P:GLN73 4.6 32.4 0.7
C1 P:13P302 4.7 28.4 0.7
CZ P:PHE76 5.0 18.8 1.0

Reference:

A.C.Joerger, C.Mueller-Dieckmann, G.E.Schulz. Structures of L-Fuculose-1-Phosphate Aldolase Mutants Outlining Motions During Catalysis J.Mol.Biol. V. 303 531 2000.
ISSN: ISSN 0022-2836
PubMed: 11054289
DOI: 10.1006/JMBI.2000.4153
Page generated: Fri Sep 25 21:22:36 2020
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