Zinc in PDB 2v9f: L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-A273S)

All present enzymatic activity of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-A273S):
4.1.2.19;

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-A273S), PDB code: 2v9f 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)	24.99 / 2.10
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	92.832, 92.832, 77.070, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / 22.9

The binding sites of Zinc atom in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-A273S) (pdb code 2v9f). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-A273S), PDB code: 2v9f:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-A273S)


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-A273S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1279 b:21.5 occ:1.00 NE2 A:HIS143 2.1 16.6 1.0 NE2 A:HIS141 2.2 18.4 1.0 NE2 A:HIS212 2.2 20.2 1.0 O A:ACT1275 2.3 32.5 1.0 OXT A:ACT1275 2.4 34.9 1.0 C A:ACT1275 2.6 30.2 1.0 CD2 A:HIS212 2.9 18.3 1.0 CE1 A:HIS143 3.0 16.0 1.0 CD2 A:HIS141 3.0 16.4 1.0 CD2 A:HIS143 3.1 16.5 1.0 CE1 A:HIS141 3.2 17.3 1.0 CE1 A:HIS212 3.3 17.8 1.0 ND1 A:HIS143 4.1 20.7 1.0 CG A:HIS212 4.2 18.8 1.0 CH3 A:ACT1275 4.2 30.9 1.0 N A:GLY31 4.2 31.5 1.0 CG A:HIS143 4.2 17.9 1.0 CG A:HIS141 4.2 19.5 1.0 ND1 A:HIS141 4.3 18.3 1.0 ND1 A:HIS212 4.3 19.5 1.0 CA A:GLY31 4.8 32.3 1.0 CZ3 A:TRP209 4.9 21.8 1.0 ND2 A:ASN32 4.9 28.9 1.0 CA A:GLY30 4.9 32.0 1.0 C A:GLY30 4.9 32.5 1.0 CE3 A:TRP209 5.0 16.5 1.0

Zinc binding site 2 out of 3 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-A273S)


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-A273S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1280 b:34.3 occ:1.00 OE1 A:GLU27 2.0 36.1 1.0 ND1 A:HIS143 2.1 20.7 1.0 CE1 A:HIS143 3.0 16.0 1.0 CG A:HIS143 3.1 17.9 1.0 CD A:GLU27 3.2 39.6 1.0 CB A:HIS143 3.5 20.7 1.0 O A:HOH2090 3.6 21.9 1.0 CG A:GLU27 3.9 36.0 1.0 OE2 A:GLU27 4.1 43.5 1.0 NE2 A:HIS143 4.1 16.6 1.0 CD2 A:HIS143 4.2 16.5 1.0 CA A:GLY30 4.5 32.0 1.0

Zinc binding site 3 out of 3 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli ( Mutant E192A-K248W-A273S)


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-A273S) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1281 b:24.8 occ:1.00 O A:ACT1276 2.0 26.7 1.0 O A:HOH2127 2.0 20.5 1.0 NE2 A:HIS46 2.1 20.5 1.0 C A:ACT1276 2.8 25.2 1.0 OXT A:ACT1276 2.9 26.9 1.0 CD2 A:HIS46 2.9 19.3 1.0 CE1 A:HIS46 3.2 21.5 1.0 CG A:HIS46 4.1 21.4 1.0 ND1 A:HIS46 4.2 22.4 1.0 CH3 A:ACT1276 4.2 27.8 1.0 O A:HOH2019 4.8 36.6 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