Zinc in PDB 2v9g: L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- L84W-E192A)

All present enzymatic activity of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- L84W-E192A):
4.1.2.19;

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- L84W-E192A), PDB code: 2v9g 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)	14.96 / 2.70
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	87.902, 100.825, 270.600, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 25.2

The binding sites of Zinc atom in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- L84W-E192A) (pdb code 2v9g). 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 Q6Y- L84W-E192A), PDB code: 2v9g:
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 Q6Y- L84W-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 Q6Y- L84W-E192A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1276 b:33.9 occ:1.00 O A:HOH2020 2.1 29.8 0.5 NE2 A:HIS212 2.1 33.1 1.0 NE2 A:HIS141 2.1 22.6 1.0 NE2 A:HIS143 2.4 24.4 1.0 O3 A:TLA1275 2.5 39.7 0.5 O2 A:TLA1275 2.9 40.7 0.5 O1 A:TLA1275 3.0 31.6 0.5 CD2 A:HIS212 3.1 32.1 1.0 CE1 A:HIS212 3.1 32.9 1.0 CD2 A:HIS141 3.1 23.6 1.0 CE1 A:HIS141 3.1 24.3 1.0 CD2 A:HIS143 3.3 29.3 1.0 CE1 A:HIS143 3.3 29.0 1.0 C2 A:TLA1275 3.4 37.3 0.5 C3 A:TLA1275 3.4 40.0 0.5 C1 A:TLA1275 3.5 36.8 0.5 O4 A:TLA1275 3.9 44.1 0.5 ND1 A:HIS212 4.2 33.8 1.0 C4 A:TLA1275 4.2 42.6 0.5 CG A:HIS212 4.2 31.9 1.0 ND1 A:HIS141 4.2 23.5 1.0 CG A:HIS141 4.2 24.4 1.0 N A:GLY31 4.3 44.8 1.0 ND1 A:HIS143 4.5 32.3 1.0 CG A:HIS143 4.5 31.8 1.0 O11 A:TLA1275 4.6 34.3 0.5 OE1 A:GLU117 4.7 37.2 1.0 CA A:GLY31 4.9 38.8 1.0 CZ3 A:TRP209 4.9 33.1 1.0

Zinc binding site 2 out of 4 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- L84W-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 Q6Y- L84W-E192A) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1277 b:33.3 occ:1.00 NE2 B:HIS212 2.2 32.4 1.0 NE2 B:HIS143 2.3 23.3 1.0 NE2 B:HIS141 2.3 23.2 1.0 O11 B:TLA1275 2.8 54.7 0.7 CE1 B:HIS143 3.1 25.4 1.0 CE1 B:HIS212 3.2 33.0 1.0 CD2 B:HIS141 3.2 23.5 1.0 CD2 B:HIS212 3.2 32.3 1.0 CD2 B:HIS143 3.3 22.6 1.0 CE1 B:HIS141 3.4 24.8 1.0 O1 B:TLA1275 3.4 47.5 0.7 C1 B:TLA1275 3.5 51.6 0.7 OE2 C:GLU171 3.5 58.7 1.0 CD C:GLU171 4.0 56.1 1.0 N B:GLY31 4.2 34.2 1.0 ND1 B:HIS143 4.3 26.5 1.0 ND1 B:HIS212 4.3 32.8 1.0 CG B:HIS212 4.4 30.9 1.0 CG B:HIS141 4.4 26.2 1.0 OE1 C:GLU171 4.4 61.3 1.0 CG B:HIS143 4.4 25.2 1.0 ND1 B:HIS141 4.4 24.2 1.0 CG C:GLU171 4.7 53.5 1.0 CA B:GLY31 4.9 34.8 1.0 C2 B:TLA1275 4.9 52.4 0.7 CA B:GLY30 5.0 32.0 1.0

Zinc binding site 3 out of 4 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- L84W-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 Q6Y- L84W-E192A) within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1276 b:39.5 occ:1.00 NE2 C:HIS212 2.1 36.0 1.0 NE2 C:HIS141 2.2 22.4 1.0 O11 C:TLA1275 2.4 30.8 0.5 NE2 C:HIS143 2.4 22.9 1.0 OE1 D:GLU171 2.9 62.1 1.0 CE1 C:HIS212 3.1 36.9 1.0 C1 C:TLA1275 3.1 32.3 0.5 CD2 C:HIS141 3.1 26.5 1.0 CD2 C:HIS212 3.1 34.9 1.0 CE1 C:HIS141 3.2 24.6 1.0 CE1 C:HIS143 3.3 23.1 1.0 CD2 C:HIS143 3.4 26.1 1.0 O1 C:TLA1275 3.7 31.9 0.5 C2 C:TLA1275 4.0 33.6 0.5 O2 C:TLA1275 4.1 35.7 0.5 CD D:GLU171 4.1 57.5 1.0 ND1 C:HIS212 4.2 35.6 1.0 CG C:HIS212 4.3 33.2 1.0 CG C:HIS141 4.3 27.3 1.0 ND1 C:HIS141 4.3 27.2 1.0 N C:GLY31 4.3 38.5 1.0 ND1 C:HIS143 4.5 27.1 1.0 CG C:HIS143 4.5 26.4 1.0 CG D:GLU171 4.9 51.5 1.0 CZ3 C:TRP209 5.0 35.5 1.0

Zinc binding site 4 out of 4 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- L84W-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 Q6Y- L84W-E192A) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1276 b:30.4 occ:1.00 NE2 D:HIS212 2.1 32.8 1.0 NE2 D:HIS141 2.2 24.4 1.0 O D:HOH2015 2.4 53.9 1.0 NE2 D:HIS143 2.4 31.7 1.0 O2 D:TLA1275 2.7 35.0 0.5 C1 D:TLA1275 2.8 31.1 0.5 O11 D:TLA1275 3.0 27.6 0.5 CD2 D:HIS212 3.0 30.2 1.0 CE1 D:HIS212 3.1 34.4 1.0 O1 D:TLA1275 3.1 30.2 0.5 CD2 D:HIS141 3.2 24.6 1.0 CE1 D:HIS141 3.2 23.8 1.0 C2 D:TLA1275 3.3 32.0 0.5 CE1 D:HIS143 3.3 29.6 1.0 CD2 D:HIS143 3.4 30.0 1.0 ND1 D:HIS212 4.1 33.1 1.0 CG D:HIS212 4.2 29.4 1.0 N D:GLY31 4.3 41.1 1.0 ND1 D:HIS141 4.3 23.2 1.0 CG D:HIS141 4.3 22.4 1.0 ND1 D:HIS143 4.5 31.9 1.0 CG D:HIS143 4.5 28.9 1.0 C3 D:TLA1275 4.6 33.9 0.5 O D:HOH2027 4.6 26.3 1.0 O3 D:TLA1275 4.7 32.5 0.5 OE1 D:GLU117 4.9 51.7 1.0 CA D:GLY31 4.9 37.0 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