Zinc in PDB 2uyu: L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A)

All present enzymatic activity of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A):
4.1.2.19;

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A), PDB code: 2uyu was solved by D.Grueninger, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 1.96
Space group	P 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	87.097, 87.097, 170.340, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 24.5

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A) also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Zinc atom in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A) (pdb code 2uyu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A), PDB code: 2uyu:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1275 b:26.2 occ:1.00 NE2 A:HIS212 2.0 20.1 1.0 NE2 A:HIS141 2.1 18.0 1.0 NE2 A:HIS143 2.2 14.2 1.0 O A:HOH2167 2.6 37.1 1.0 CE1 A:HIS212 3.0 17.1 1.0 CD2 A:HIS212 3.1 18.8 1.0 CD2 A:HIS141 3.1 21.9 1.0 CE1 A:HIS143 3.1 15.6 1.0 CE1 A:HIS141 3.1 24.1 1.0 CD2 A:HIS143 3.2 20.4 1.0 ND1 A:HIS212 4.1 20.6 1.0 CG A:HIS212 4.2 21.1 1.0 ND1 A:HIS141 4.2 18.2 1.0 ND1 A:HIS143 4.3 15.5 1.0 CG A:HIS141 4.3 19.7 1.0 CG A:HIS143 4.3 17.1 1.0 N A:GLY31 4.5 23.4 1.0 CZ3 A:TRP209 4.7 27.6 1.0 CA A:GLY30 4.9 24.1 1.0 C A:GLY30 5.0 24.8 1.0 O A:HIS212 5.0 17.6 1.0

Zinc binding site 2 out of 2 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A) within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn1275 b:25.4 occ:1.00 O E:HOH2174 1.6 34.3 1.0 NE2 E:HIS212 2.0 19.6 1.0 NE2 E:HIS141 2.1 17.6 1.0 NE2 E:HIS143 2.2 13.7 1.0 CD2 E:HIS212 3.0 19.4 1.0 CE1 E:HIS212 3.0 18.1 1.0 CE1 E:HIS141 3.0 23.8 1.0 CD2 E:HIS143 3.1 21.1 1.0 CD2 E:HIS141 3.1 21.6 1.0 CE1 E:HIS143 3.2 16.0 1.0 O E:HOH2173 3.3 49.5 1.0 ND1 E:HIS212 4.1 21.2 1.0 CG E:HIS212 4.2 22.0 1.0 ND1 E:HIS141 4.2 18.7 1.0 CG E:HIS141 4.2 20.1 1.0 CG E:HIS143 4.3 17.5 1.0 ND1 E:HIS143 4.3 15.4 1.0 N E:GLY31 4.5 23.3 1.0 CZ3 E:TRP209 4.7 27.2 1.0 CA E:GLY30 5.0 23.7 1.0 C E:GLY30 5.0 25.1 1.0

D.Grueninger, N.Treiber, M.O.P.Ziegler, J.W.A.Koetter, M.-S.Schulze, G.E.Schulz. Designed Protein-Protein Association. Science V. 319 206 2008.
ISSN: ISSN 0036-8075
PubMed: 18187656
DOI: 10.1126/SCIENCE.1150421