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

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

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant E192A), PDB code: 1ojr was solved by M.Kroemer, I.Merkel, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.43 / 1.35
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	108.024, 108.024, 57.166, 90.00, 90.00, 90.00
R / Rfree (%)	11.1 / 14.2

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

Zinc binding site 1 out of 1 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant 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 E192A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1275 b:8.8 occ:1.00 O3 A:PO41278 1.9 12.5 0.5 O2 A:2HA1277 2.0 16.7 0.5 NE2 A:HIS212 2.0 7.8 1.0 NE2 A:HIS143 2.1 7.9 1.0 NE2 A:HIS141 2.1 7.1 1.0 O1 A:2HA1277 2.4 10.2 0.5 C2 A:2HA1277 2.7 19.5 0.5 P A:PO41278 2.8 13.2 0.5 O1 A:PO41278 2.8 14.1 0.5 O A:HOH2503 2.9 23.5 1.0 C1 A:2HA1277 2.9 19.1 0.5 CD2 A:HIS212 2.9 8.3 1.0 CE1 A:HIS143 3.1 7.7 1.0 CD2 A:HIS141 3.1 8.0 1.0 CD2 A:HIS143 3.1 7.5 1.0 CE1 A:HIS212 3.1 7.2 1.0 CE1 A:HIS141 3.1 9.6 1.0 O4 A:PO41278 3.6 18.4 0.5 O2 A:PO41278 4.0 14.9 0.5 C3 A:2HA1277 4.1 22.6 0.5 CG A:HIS212 4.1 7.1 1.0 N A:GLY31 4.2 10.1 1.0 ND1 A:HIS212 4.2 7.5 1.0 ND1 A:HIS143 4.2 7.4 1.0 ND1 A:HIS141 4.2 9.0 1.0 CG A:HIS143 4.2 7.2 1.0 CG A:HIS141 4.3 8.0 1.0 O3 A:2HA1277 4.7 31.7 0.5 O A:HOH2507 4.7 27.2 1.0 CA A:GLY31 4.8 8.7 1.0 CZ3 A:TRP209 4.9 10.3 1.0 CA A:GLY30 4.9 9.2 1.0

M.Kroemer, I.Merkel, G.E.Schulz. Structure and Catalytic Mechanism of L-Rhamnulose-1-Phosphate Aldolase. Biochemistry V. 42 10560 2003.
ISSN: ISSN 0006-2960
PubMed: 12962479
DOI: 10.1021/BI0349266