Zinc in PDB 2v9i: L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-L274STOP)

All present enzymatic activity of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-L274STOP):
4.1.2.19;

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-L274STOP), PDB code: 2v9i 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)	14.94 / 1.80
Space group	P 4
Cell size a, b, c (Å), α, β, γ (°)	85.207, 85.207, 90.535, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 23.8

The binding sites of Zinc atom in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-L274STOP) (pdb code 2v9i). 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 E192A-K248W-L274STOP), PDB code: 2v9i:
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 E192A-K248W-L274STOP)


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-K248W-L274STOP) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1275 b:25.9 occ:1.00 NE2 A:HIS143 2.0 23.8 1.0 NE2 A:HIS141 2.1 22.2 1.0 NE2 A:HIS212 2.1 25.4 1.0 O A:HOH2206 2.2 25.2 1.0 O A:HOH2205 2.7 59.9 1.0 CD2 A:HIS212 2.9 20.6 1.0 CE1 A:HIS143 3.0 22.0 1.0 CD2 A:HIS143 3.0 19.9 1.0 CD2 A:HIS141 3.0 23.3 1.0 CE1 A:HIS141 3.1 25.2 1.0 CE1 A:HIS212 3.2 20.7 1.0 N A:GLY31 4.0 25.7 1.0 ND1 A:HIS143 4.1 24.6 1.0 CG A:HIS143 4.1 23.2 1.0 CG A:HIS212 4.1 20.8 1.0 ND1 A:HIS141 4.2 22.9 1.0 CG A:HIS141 4.2 22.1 1.0 ND1 A:HIS212 4.2 20.9 1.0 CA A:GLY31 4.7 24.9 1.0 CZ3 A:TRP209 4.8 28.1 1.0 CE3 A:TRP209 4.9 27.4 1.0 C A:GLY30 4.9 27.3 1.0 CA A:GLY30 4.9 25.6 1.0

Zinc binding site 2 out of 4 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-L274STOP)


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-K248W-L274STOP) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1276 b:31.2 occ:1.00 OE2 A:GLU200 1.9 25.7 1.0 NE2 A:HIS204 2.1 26.0 1.0 CD2 A:HIS204 2.8 24.2 1.0 CD A:GLU200 2.9 28.1 1.0 OE1 A:GLU200 3.2 29.2 1.0 CE1 A:HIS204 3.3 24.2 1.0 CG A:HIS204 4.1 24.1 1.0 CB A:LYS203 4.2 24.0 1.0 CA A:GLY181 4.2 26.9 1.0 ND1 A:HIS204 4.3 22.9 1.0 CG A:GLU200 4.3 27.1 1.0 OG1 A:THR158 4.5 25.8 1.0 CB A:GLU200 4.7 24.8 1.0 CG A:LYS203 4.7 25.0 1.0 CG2 A:THR158 4.8 23.7 1.0 CA A:GLU200 4.8 24.5 1.0 O A:GLU200 4.9 25.4 1.0

Zinc binding site 3 out of 4 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-L274STOP)


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 E192A-K248W-L274STOP) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1277 b:30.8 occ:1.00 OE1 B:GLU200 2.0 27.5 1.0 NE2 A:HIS46 2.1 25.2 1.0 NE2 B:HIS204 2.1 24.5 1.0 OD2 A:ASP47 2.2 21.9 1.0 OD1 A:ASP47 2.7 26.3 1.0 CG A:ASP47 2.7 22.1 1.0 CD2 B:HIS204 2.8 22.7 1.0 CD B:GLU200 2.9 28.6 1.0 CD2 A:HIS46 3.0 21.3 1.0 CE1 A:HIS46 3.0 21.6 1.0 OE2 B:GLU200 3.2 30.6 1.0 CE1 B:HIS204 3.3 24.3 1.0 CG B:HIS204 4.1 24.2 1.0 ND1 A:HIS46 4.1 20.7 1.0 CG A:HIS46 4.1 23.5 1.0 CB B:LYS203 4.1 23.3 1.0 CB A:ASP47 4.2 21.6 1.0 CA B:GLY181 4.2 26.2 1.0 ND1 B:HIS204 4.2 23.0 1.0 CG B:GLU200 4.3 28.1 1.0 O A:HOH2052 4.3 46.2 1.0 OG1 B:THR158 4.5 25.7 1.0 CB B:GLU200 4.7 25.6 1.0 O A:HOH2049 4.7 43.2 1.0 CG B:LYS203 4.8 24.7 1.0 CG2 B:THR158 4.8 24.7 1.0 N A:ASP47 4.8 21.3 1.0 CA B:GLU200 4.8 24.8 1.0 O B:GLU200 4.9 26.2 1.0 CA A:ASP47 4.9 22.8 1.0

Zinc binding site 4 out of 4 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-L274STOP)


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 E192A-K248W-L274STOP) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1275 b:25.9 occ:1.00 NE2 B:HIS143 2.0 22.0 1.0 NE2 B:HIS141 2.0 24.6 1.0 O B:HOH2207 2.2 21.5 1.0 NE2 B:HIS212 2.2 21.8 1.0 CE1 B:HIS143 2.9 21.4 1.0 CD2 B:HIS212 3.0 21.4 1.0 CD2 B:HIS141 3.0 24.7 1.0 CD2 B:HIS143 3.0 21.4 1.0 CE1 B:HIS141 3.1 26.9 1.0 CE1 B:HIS212 3.3 23.9 1.0 N B:GLY31 4.0 25.3 1.0 ND1 B:HIS143 4.1 23.8 1.0 CG B:HIS143 4.2 21.5 1.0 ND1 B:HIS141 4.2 24.6 1.0 CG B:HIS212 4.2 22.1 1.0 CG B:HIS141 4.2 24.1 1.0 O B:HOH2154 4.3 49.8 1.0 ND1 B:HIS212 4.3 22.4 1.0 CA B:GLY31 4.7 25.4 1.0 CZ3 B:TRP209 4.8 27.7 1.0 OE1 B:GLU117 4.9 45.1 1.0 CA B:GLY30 4.9 24.7 1.0 C B:GLY30 4.9 26.3 1.0 CE3 B:TRP209 4.9 27.5 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