Zinc in PDB 2v2a: L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant E192A- K248G-R253A-E254A)

All present enzymatic activity of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant E192A- K248G-R253A-E254A):
4.1.2.19;

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant E192A- K248G-R253A-E254A), PDB code: 2v2a 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)	19.90 / 1.75
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	106.302, 106.302, 56.439, 90.00, 90.00, 90.00
R / Rfree (%)	14.7 / 17.2

The binding sites of Zinc atom in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant E192A- K248G-R253A-E254A) (pdb code 2v2a). 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 E192A- K248G-R253A-E254A), PDB code: 2v2a:
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 E192A- K248G-R253A-E254A)


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 E192A- K248G-R253A-E254A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1275 b:6.9 occ:1.00 NE2 A:HIS141 2.1 6.7 1.0 NE2 A:HIS212 2.1 7.0 1.0 NE2 A:HIS143 2.1 7.0 1.0 O2 A:13P1277 2.1 9.6 0.4 O2 A:13P1277 2.2 8.6 0.4 O3 A:13P1277 2.6 4.4 0.4 C2 A:13P1277 2.9 12.0 0.4 CD2 A:HIS212 2.9 8.5 1.0 CE1 A:HIS143 3.0 6.5 1.0 CD2 A:HIS141 3.0 6.8 1.0 CE1 A:HIS141 3.1 7.8 1.0 C3 A:13P1277 3.1 10.0 0.4 C2 A:13P1277 3.1 8.5 0.4 CD2 A:HIS143 3.1 6.4 1.0 CE1 A:HIS212 3.2 8.0 1.0 O A:HOH2275 3.2 30.4 1.0 C3 A:13P1277 3.3 6.3 0.4 O3 A:13P1277 3.5 12.1 0.4 N A:GLY31 4.1 9.6 1.0 CG A:HIS212 4.1 8.0 1.0 ND1 A:HIS141 4.2 7.2 1.0 ND1 A:HIS143 4.2 7.3 1.0 CG A:HIS141 4.2 6.7 1.0 ND1 A:HIS212 4.2 8.2 1.0 CG A:HIS143 4.2 6.5 1.0 C1 A:13P1277 4.4 10.9 0.4 C1 A:13P1277 4.5 7.9 0.4 C A:GLY30 4.6 10.0 0.4 CA A:GLY31 4.7 9.3 1.0 CA A:GLY30 4.8 9.8 0.4 O A:HOH2277 4.8 44.1 1.0 CZ3 A:TRP209 4.9 8.8 1.0 CA A:GLY30 4.9 8.4 0.6 C A:GLY30 5.0 8.2 0.6

Zinc binding site 2 out of 2 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant E192A- K248G-R253A-E254A)


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 E192A- K248G-R253A-E254A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1276 b:17.4 occ:0.50 O A:HOH2273 2.2 16.6 1.0 ND1 A:HIS46 2.5 20.1 1.0 O A:HOH2272 3.3 36.0 1.0 CG A:HIS46 3.4 18.4 1.0 CE1 A:HIS46 3.5 19.4 1.0 O A:HIS46 3.6 18.4 1.0 CB A:HIS46 3.6 17.5 1.0 C A:HIS46 3.8 18.2 1.0 CA A:HIS46 4.3 17.6 1.0 N A:ASP47 4.4 18.8 0.5 CD2 A:HIS46 4.6 18.8 1.0 NE2 A:HIS46 4.6 19.1 1.0 O A:HOH2090 4.7 31.7 1.0 OD1 A:ASP47 4.7 23.6 0.5 CA A:ASP47 4.8 20.2 0.5 CA A:ASP47 4.9 21.4 0.5

D.Grueninger, G.E.Schulz. Antenna Domain Mobility and Enzymatic Reaction of L-Rhamnulose-1-Phosphate Aldolase. Biochemistry V. 47 607 2008.
ISSN: ISSN 0006-2960
PubMed: 18085797
DOI: 10.1021/BI7012799