Zinc in PDB 2v2b: L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E117S-E192A-K248G-R253A-E254A)

All present enzymatic activity of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E117S-E192A-K248G-R253A-E254A):
4.1.2.19;

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E117S-E192A-K248G-R253A-E254A), PDB code: 2v2b 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)	36.35 / 1.5
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	84.230, 84.230, 91.747, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 18.4

The binding sites of Zinc atom in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E117S-E192A-K248G-R253A-E254A) (pdb code 2v2b). 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 E117S-E192A-K248G-R253A-E254A), PDB code: 2v2b:
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 E117S-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 E117S-E192A-K248G-R253A-E254A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1274 b:11.2 occ:1.00 OXT A:ACT1276 1.7 22.8 1.0 NE2 A:HIS141 2.1 8.7 1.0 NE2 A:HIS212 2.1 7.9 1.0 NE2 A:HIS143 2.1 8.7 1.0 O A:HOH2212 2.5 21.9 1.0 C A:ACT1276 2.6 21.4 1.0 O A:ACT1276 2.8 19.2 1.0 CD2 A:HIS212 2.9 8.6 1.0 CE1 A:HIS141 3.0 12.3 1.0 CD2 A:HIS141 3.1 10.0 1.0 CE1 A:HIS143 3.1 10.2 1.0 CD2 A:HIS143 3.1 11.0 1.0 CE1 A:HIS212 3.2 9.3 1.0 O A:HOH2213 3.4 44.9 1.0 CH3 A:ACT1276 4.0 21.4 1.0 ND1 A:HIS141 4.1 12.6 1.0 CG A:HIS212 4.2 10.7 1.0 CG A:HIS141 4.2 12.7 1.0 ND1 A:HIS143 4.2 9.5 1.0 ND1 A:HIS212 4.3 13.5 1.0 CG A:HIS143 4.3 9.1 1.0 O A:HOH2125 4.4 33.2 1.0 N A:GLY31 4.4 11.1 1.0 CZ3 A:TRP209 5.0 22.1 1.0

Zinc binding site 2 out of 2 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E117S-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 E117S-E192A-K248G-R253A-E254A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1275 b:22.5 occ:1.00 OE1 A:GLU200 1.4 5.9 1.0 NE2 A:HIS204 2.0 2.0 1.0 CD A:GLU200 2.3 12.4 1.0 OE2 A:GLU200 2.5 16.9 1.0 CE1 A:HIS204 3.0 9.7 1.0 CD2 A:HIS204 3.0 8.8 1.0 CG A:GLU200 3.8 11.8 1.0 ND1 A:HIS204 4.1 9.2 1.0 CG A:HIS204 4.1 9.9 1.0 CB A:LYS203 4.2 12.9 0.5 CB A:LYS203 4.2 12.6 0.5 O A:HOH2160 4.4 36.8 1.0 CD A:LYS203 4.4 11.2 0.5 OG1 A:THR158 4.5 19.7 1.0 CA A:GLY181 4.5 13.9 1.0 CG A:LYS203 4.5 13.3 0.5 CG A:LYS203 4.6 12.3 0.5 CG2 A:THR158 4.6 17.5 1.0 CB A:GLU200 4.7 12.1 1.0 CB A:THR158 5.0 18.4 1.0 CA A:GLU200 5.0 11.7 1.0

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