Zinc in PDB 2v9l: L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A)

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

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A), PDB code: 2v9l 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)	10.00 / 1.23
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	107.059, 107.059, 57.161, 90.00, 90.00, 90.00
R / Rfree (%)	9 / 12.2

The binding sites of Zinc atom in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A) (pdb code 2v9l). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- E192A), PDB code: 2v9l:

Zinc binding site 1 out of 1 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant Q6Y- 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- E192A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1275 b:10.1 occ:1.00 NE2 A:HIS212 2.0 10.0 1.0 NE2 A:HIS141 2.0 9.4 1.0 NE2 A:HIS143 2.0 9.0 1.0 O1 A:PO41276 2.1 17.2 0.6 O4 A:PO41276 2.4 25.8 0.6 P A:PO41276 2.5 28.1 0.6 O A:HOH2535 2.5 12.7 0.2 O2 A:PO41276 2.8 32.5 0.6 CD2 A:HIS212 2.9 9.7 1.0 HD2 A:HIS212 3.0 11.7 1.0 CE1 A:HIS141 3.0 9.8 1.0 CE1 A:HIS143 3.1 8.7 1.0 CD2 A:HIS143 3.1 8.8 1.0 CD2 A:HIS141 3.1 9.7 1.0 CE1 A:HIS212 3.1 10.8 1.0 HE1 A:HIS141 3.2 11.8 1.0 HE1 A:HIS143 3.2 10.5 1.0 HD2 A:HIS143 3.3 10.5 1.0 HD2 A:HIS141 3.3 11.7 1.0 HE1 A:HIS212 3.4 13.0 1.0 H A:GLY31 3.4 12.4 0.5 O3 A:PO41276 4.1 16.9 0.6 HA2 A:GLY30 4.2 12.6 0.5 CG A:HIS212 4.2 9.8 1.0 HA2 A:GLY30 4.2 11.1 0.5 O A:HOH2354 4.2 40.8 1.0 ND1 A:HIS212 4.2 10.7 1.0 ND1 A:HIS143 4.2 9.4 1.0 ND1 A:HIS141 4.2 9.8 1.0 CG A:HIS143 4.2 8.2 1.0 N A:GLY31 4.2 10.3 0.5 CG A:HIS141 4.2 9.2 1.0 HZ3 A:TRP209 4.3 13.1 1.0 HD22 A:ASN32 4.4 14.2 1.0 HA2 A:GLY31 4.5 14.4 0.5 HE3 A:TRP209 4.6 13.4 1.0 N A:GLY31 4.7 9.9 0.5 C A:GLY30 4.7 8.8 0.5 CA A:GLY30 4.8 10.5 0.5 HA3 A:GLY30 4.8 12.6 0.5 H A:GLY31 4.8 11.9 0.5 HG3 A:GLU117 4.9 17.6 1.0 CZ3 A:TRP209 4.9 10.9 1.0 CA A:GLY30 4.9 9.2 0.5 HD1 A:HIS143 5.0 11.3 1.0 HD1 A:HIS212 5.0 12.8 1.0 HD1 A:HIS141 5.0 11.7 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