Zinc in PDB 1fa5: Crystal Structure of the Zn(II)-Bound Glyoxalase I of Escherichia Coli

All present enzymatic activity of Crystal Structure of the Zn(II)-Bound Glyoxalase I of Escherichia Coli:
4.4.1.5;

The structure of Crystal Structure of the Zn(II)-Bound Glyoxalase I of Escherichia Coli, PDB code: 1fa5 was solved by M.M.He, S.L.Clugston, J.F.Honek, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.240, 57.170, 46.990, 90.00, 95.36, 90.00
R / Rfree (%)	18.6 / 26

The binding sites of Zinc atom in the Crystal Structure of the Zn(II)-Bound Glyoxalase I of Escherichia Coli (pdb code 1fa5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Zn(II)-Bound Glyoxalase I of Escherichia Coli, PDB code: 1fa5:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Zn(II)-Bound Glyoxalase I of Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Zn(II)-Bound Glyoxalase I of Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1200 b:18.7 occ:1.00 NE2 A:HIS5 2.1 11.8 1.0 OE1 A:GLU56 2.1 21.2 1.0 NE2 B:HIS74 2.1 10.2 1.0 O B:HOH216 2.1 18.3 1.0 OE1 B:GLU122 2.2 19.3 1.0 CE1 B:HIS74 3.0 9.9 1.0 CE1 A:HIS5 3.1 11.5 1.0 CD2 A:HIS5 3.1 11.5 1.0 CD A:GLU56 3.1 28.4 1.0 CD B:GLU122 3.2 29.5 1.0 CD2 B:HIS74 3.2 13.4 1.0 O B:HOH237 3.4 43.1 1.0 OE2 A:GLU56 3.6 18.8 1.0 OE2 B:GLU122 3.7 29.1 1.0 ND1 A:HIS5 4.2 11.0 1.0 ND1 B:HIS74 4.2 10.6 1.0 CG A:HIS5 4.2 8.9 1.0 O A:HOH1236 4.3 32.1 1.0 CG B:HIS74 4.3 10.3 1.0 CB B:ALA76 4.3 10.9 1.0 CB A:MET7 4.4 12.2 1.0 CG B:GLU122 4.4 12.7 1.0 CG A:GLU56 4.5 11.2 1.0 CB B:GLU122 4.6 14.4 1.0 CB A:GLU56 4.7 14.9 1.0 CG A:MET7 4.8 13.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Zn(II)-Bound Glyoxalase I of Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Zn(II)-Bound Glyoxalase I of Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1201 b:17.3 occ:1.00 O B:HOH204 1.9 14.9 1.0 NE2 B:HIS5 2.1 10.8 1.0 OE1 B:GLU56 2.1 15.0 1.0 NE2 A:HIS74 2.1 10.0 1.0 OE1 A:GLU122 2.5 29.0 1.0 CE1 A:HIS74 2.9 9.8 1.0 CE1 B:HIS5 3.0 8.4 1.0 CD B:GLU56 3.1 15.6 1.0 CD2 B:HIS5 3.1 11.7 1.0 CD2 A:HIS74 3.3 13.8 1.0 CD A:GLU122 3.5 25.9 1.0 OE2 B:GLU56 3.5 19.9 1.0 OE2 A:GLU122 4.0 27.9 1.0 O B:HOH213 4.0 89.9 1.0 ND1 B:HIS5 4.1 11.4 1.0 ND1 A:HIS74 4.1 11.0 1.0 CG B:HIS5 4.2 9.2 1.0 CB A:ALA76 4.3 9.6 1.0 CB B:MET7 4.3 8.2 1.0 CG A:HIS74 4.3 10.9 1.0 CG B:GLU56 4.4 7.0 1.0 O B:HOH240 4.4 14.9 1.0 CG B:MET7 4.6 7.7 1.0 CB B:GLU56 4.7 6.5 1.0 CG A:GLU122 4.7 14.8 1.0 CB A:GLU122 4.8 10.9 1.0

M.M.He, S.L.Clugston, J.F.Honek, B.W.Matthews. Determination of the Structure of Escherichia Coli Glyoxalase I Suggests A Structural Basis For Differential Metal Activation. Biochemistry V. 39 8719 2000.
ISSN: ISSN 0006-2960
PubMed: 10913283
DOI: 10.1021/BI000856G