Zinc in PDB 1dzu: L-Fuculose-1-Phosphate Aldolase From Escherichia Coli Mutant T26A

All present enzymatic activity of L-Fuculose-1-Phosphate Aldolase From Escherichia Coli Mutant T26A:
4.1.2.17;

The structure of L-Fuculose-1-Phosphate Aldolase From Escherichia Coli Mutant T26A, PDB code: 1dzu 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 / 2.09
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	93.800, 93.800, 43.000, 90.00, 90.00, 90.00
R / Rfree (%)	15 / 20.7

The binding sites of Zinc atom in the L-Fuculose-1-Phosphate Aldolase From Escherichia Coli Mutant T26A (pdb code 1dzu). 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 T26A, PDB code: 1dzu:

Zinc binding site 1 out of 1 in the L-Fuculose-1-Phosphate Aldolase From Escherichia Coli Mutant T26A


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 T26A within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn999 b:10.9 occ:1.00 NE2 P:HIS94 2.0 11.4 1.0 OE2 P:GLU73 2.1 13.5 1.0 NE2 P:HIS92 2.1 8.2 1.0 NE2 P:HIS155 2.1 10.7 1.0 OE1 P:GLU73 2.6 13.3 1.0 CD P:GLU73 2.7 12.2 1.0 CD2 P:HIS94 2.9 11.4 1.0 CE1 P:HIS92 3.0 7.7 1.0 CD2 P:HIS155 3.0 10.6 1.0 CE1 P:HIS94 3.1 12.0 1.0 CE1 P:HIS155 3.2 9.6 1.0 CD2 P:HIS92 3.2 9.1 1.0 O P:HOH2012 4.0 20.8 1.0 CG P:HIS94 4.1 12.6 1.0 ND1 P:HIS92 4.2 6.3 1.0 CG P:GLU73 4.2 10.8 1.0 ND1 P:HIS94 4.2 12.3 1.0 CG P:HIS155 4.2 9.0 1.0 ND1 P:HIS155 4.2 8.8 1.0 CG P:HIS92 4.3 7.4 1.0 CZ P:PHE76 4.5 13.9 1.0 O P:ALA27 4.8 28.8 1.0 CB P:GLU73 5.0 10.7 1.0 CE2 P:PHE76 5.0 13.7 1.0

A.C.Joerger, C.Gosse, W.-D.Fessner, G.E.Schulz. Catalytic Action of Fuculose 1-Phosphate Aldolase (Class II) As Derived From Structure-Directed Mutagenesis Biochemistry V. 39 6033 2000.
ISSN: ISSN 0006-2960
PubMed: 10821675
DOI: 10.1021/BI9927686