Zinc in PDB 2v9n: 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: 2v9n 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)	51.03 / 1.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	168.379, 106.417, 106.564, 90.00, 126.76, 90.00
R / Rfree (%)	16.6 / 18.7

The binding sites of Zinc atom in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A) (pdb code 2v9n). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A), PDB code: 2v9n:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 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:4.3 occ:1.00 NE2 A:HIS143 2.1 3.5 1.0 O4 A:CIT1276 2.1 4.3 1.0 NE2 A:HIS212 2.1 5.0 1.0 NE2 A:HIS141 2.2 4.0 1.0 O5 A:CIT1276 2.2 4.4 1.0 O7 A:CIT1276 2.2 4.7 1.0 C6 A:CIT1276 3.0 4.9 1.0 C3 A:CIT1276 3.0 4.4 1.0 CE1 A:HIS143 3.0 4.0 1.0 CD2 A:HIS212 3.1 4.2 1.0 C5 A:CIT1276 3.1 5.7 1.0 CD2 A:HIS143 3.1 4.5 1.0 CE1 A:HIS212 3.1 4.6 1.0 CE1 A:HIS141 3.1 5.0 1.0 CD2 A:HIS141 3.2 5.0 1.0 C4 A:CIT1276 3.5 4.6 1.0 ND1 A:HIS143 4.2 3.7 1.0 O6 A:CIT1276 4.2 6.7 1.0 O3 A:CIT1276 4.2 6.3 1.0 ND1 A:HIS212 4.2 4.5 1.0 CG A:HIS212 4.2 4.6 1.0 CG A:HIS143 4.2 3.5 1.0 ND1 A:HIS141 4.3 4.2 1.0 O2 A:CIT1276 4.3 6.6 1.0 CG A:HIS141 4.3 4.9 1.0 N A:GLY31 4.4 4.8 1.0 C2 A:CIT1276 4.4 5.1 1.0 O C:HOH2216 4.5 6.9 1.0 C1 A:CIT1276 4.8 6.2 1.0 CZ3 A:TRP209 4.9 5.9 1.0

Zinc binding site 2 out of 4 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 B:Zn1275 b:4.5 occ:1.00 NE2 B:HIS141 2.1 4.8 1.0 O5 B:CIT1276 2.1 3.9 1.0 O4 B:CIT1276 2.1 3.8 1.0 NE2 B:HIS143 2.1 4.0 1.0 NE2 B:HIS212 2.2 4.3 1.0 O7 B:CIT1276 2.3 3.7 1.0 C6 B:CIT1276 2.9 4.7 1.0 C3 B:CIT1276 3.0 4.7 1.0 CE1 B:HIS143 3.1 3.8 1.0 CE1 B:HIS141 3.1 5.7 1.0 CD2 B:HIS212 3.1 4.7 1.0 C5 B:CIT1276 3.1 5.3 1.0 CD2 B:HIS141 3.1 5.1 1.0 CE1 B:HIS212 3.2 5.4 1.0 CD2 B:HIS143 3.2 4.3 1.0 C4 B:CIT1276 3.6 4.5 1.0 O6 B:CIT1276 4.2 6.3 1.0 O3 B:CIT1276 4.2 5.2 1.0 ND1 B:HIS141 4.2 4.0 1.0 ND1 B:HIS143 4.2 4.3 1.0 O2 B:CIT1276 4.2 6.1 1.0 ND1 B:HIS212 4.3 5.1 1.0 CG B:HIS212 4.3 4.9 1.0 CG B:HIS141 4.3 4.6 1.0 CG B:HIS143 4.3 3.0 1.0 N B:GLY31 4.4 4.7 1.0 C2 B:CIT1276 4.4 5.9 1.0 O D:HOH2190 4.5 6.8 1.0 C1 B:CIT1276 4.8 7.2 1.0 CZ3 B:TRP209 4.9 5.9 1.0

Zinc binding site 3 out of 4 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 3 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A) within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1275 b:4.7 occ:1.00 O5 C:CIT1276 2.1 4.5 1.0 O3 C:CIT1276 2.1 5.8 1.0 NE2 C:HIS143 2.1 3.1 1.0 NE2 C:HIS212 2.1 4.6 1.0 NE2 C:HIS141 2.2 4.3 1.0 O7 C:CIT1276 2.2 4.8 1.0 C6 C:CIT1276 2.9 5.7 1.0 C3 C:CIT1276 3.0 5.4 1.0 C5 C:CIT1276 3.1 5.9 1.0 CE1 C:HIS143 3.1 3.7 1.0 CE1 C:HIS212 3.1 4.6 1.0 CD2 C:HIS212 3.1 5.0 1.0 CE1 C:HIS141 3.2 4.6 1.0 CD2 C:HIS143 3.2 4.4 1.0 CD2 C:HIS141 3.2 4.8 1.0 C4 C:CIT1276 3.6 4.9 1.0 O6 C:CIT1276 4.1 7.0 1.0 O4 C:CIT1276 4.2 5.0 1.0 ND1 C:HIS143 4.2 3.8 1.0 O2 C:CIT1276 4.2 7.0 1.0 ND1 C:HIS212 4.2 4.7 1.0 ND1 C:HIS141 4.3 3.9 1.0 CG C:HIS212 4.3 4.6 1.0 CG C:HIS143 4.3 2.7 1.0 CG C:HIS141 4.3 5.3 1.0 C2 C:CIT1276 4.4 6.2 1.0 N C:GLY31 4.4 4.8 1.0 O B:HOH2207 4.5 8.5 1.0 C1 C:CIT1276 4.8 7.3 1.0 CZ3 C:TRP209 4.9 6.2 1.0

Zinc binding site 4 out of 4 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 4 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1275 b:4.6 occ:1.00 NE2 D:HIS212 2.1 4.8 1.0 NE2 D:HIS141 2.1 4.4 1.0 NE2 D:HIS143 2.1 4.0 1.0 O4 D:CIT1276 2.1 4.5 1.0 O5 D:CIT1276 2.2 4.7 1.0 O7 D:CIT1276 2.3 5.2 1.0 C6 D:CIT1276 3.0 5.5 1.0 C3 D:CIT1276 3.1 5.7 1.0 CE1 D:HIS143 3.1 3.2 1.0 CE1 D:HIS141 3.1 4.7 1.0 CD2 D:HIS212 3.1 4.9 1.0 C5 D:CIT1276 3.1 4.3 1.0 CE1 D:HIS212 3.1 5.2 1.0 CD2 D:HIS141 3.1 4.8 1.0 CD2 D:HIS143 3.2 4.2 1.0 C4 D:CIT1276 3.6 5.4 1.0 O6 D:CIT1276 4.2 7.6 1.0 O3 D:CIT1276 4.2 4.7 1.0 ND1 D:HIS143 4.2 3.7 1.0 ND1 D:HIS141 4.2 3.9 1.0 ND1 D:HIS212 4.2 4.8 1.0 O2 D:CIT1276 4.2 8.5 1.0 CG D:HIS212 4.3 4.7 1.0 CG D:HIS141 4.3 4.7 1.0 CG D:HIS143 4.3 2.4 1.0 N D:GLY31 4.4 4.7 1.0 C2 D:CIT1276 4.4 6.5 1.0 O A:HOH2210 4.5 7.2 1.0 C1 D:CIT1276 4.8 6.6 1.0 CZ3 D:TRP209 4.9 6.2 1.0

D.Grueninger, N.Treiber, M.O.Ziegler, J.W.Koetter, M.S.Schulze, G.E.Schulz. Designed Protein-Protein Association. Science V. 319 206 2008.
ISSN: ESSN 1095-9203
PubMed: 18187656
DOI: 10.1126/SCIENCE.1150421