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

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

The structure of L-Fuculose-1-Phosphate Aldolase From Escherichia Coli Mutant Y113F/Y209F, PDB code: 1dzv 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 / 1.86
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	93.700, 93.700, 42.800, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 21.6

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

Zinc binding site 1 out of 1 in the L-Fuculose-1-Phosphate Aldolase From Escherichia Coli Mutant 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 Y113F/Y209F within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn999 b:20.8 occ:1.00 NE2 P:HIS92 2.1 14.5 1.0 NE2 P:HIS155 2.2 13.4 1.0 NE2 P:HIS94 2.2 21.7 1.0 OE1 P:GLU73 2.4 28.0 1.0 OE2 P:GLU73 2.6 29.0 1.0 CD P:GLU73 2.8 27.7 1.0 CD2 P:HIS155 3.0 12.4 1.0 CE1 P:HIS92 3.1 13.5 1.0 CD2 P:HIS94 3.1 19.7 1.0 CD2 P:HIS92 3.1 14.1 1.0 CE1 P:HIS155 3.3 14.4 1.0 CE1 P:HIS94 3.3 21.3 1.0 O P:HOH2041 3.5 37.3 1.0 ND1 P:HIS92 4.2 14.0 1.0 CG P:HIS92 4.2 14.0 1.0 CG P:HIS155 4.3 11.8 1.0 CG P:HIS94 4.3 20.4 1.0 CG P:GLU73 4.3 26.3 1.0 ND1 P:HIS155 4.3 13.6 1.0 ND1 P:HIS94 4.3 20.7 1.0 CZ P:PHE76 4.6 18.0 1.0 O P:ALA27 4.7 39.4 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