Zinc in PDB 2bnm: The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis.

The structure of The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis., PDB code: 2bnm was solved by K.Mcluskey, S.Cameron, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.7
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	86.363, 86.363, 221.440, 90.00, 90.00, 120.00
R / Rfree (%)	18.8 / 23

The binding sites of Zinc atom in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis. (pdb code 2bnm). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis., PDB code: 2bnm:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1199 b:26.1 occ:1.00 NE2 A:HIS138 2.0 16.9 1.0 O A:HOH2255 2.0 25.9 1.0 OE2 A:GLU142 2.0 20.6 1.0 NE2 A:HIS180 2.1 17.8 1.0 CD A:GLU142 2.7 19.7 1.0 OE1 A:GLU142 2.7 28.7 1.0 CD2 A:HIS138 2.9 20.3 1.0 CE1 A:HIS138 3.0 27.4 1.0 CE1 A:HIS180 3.0 20.5 1.0 CD2 A:HIS180 3.1 21.0 1.0 O A:HOH2267 3.5 57.5 1.0 CG A:HIS138 4.0 25.5 1.0 ND1 A:HIS138 4.1 25.9 1.0 O A:HOH2270 4.1 39.0 1.0 CG A:GLU142 4.2 16.1 1.0 O A:HOH2214 4.2 24.9 1.0 ND1 A:HIS180 4.2 19.2 1.0 CG A:HIS180 4.2 19.1 1.0 CE1 A:PHE182 4.4 18.4 0.5 ND2 A:ASN135 4.4 29.7 1.0 O1 A:SO41203 4.4 29.2 0.6 CB A:GLU142 4.6 17.1 1.0 ND2 A:ASN197 4.8 25.3 1.0 CE2 A:PHE182 4.8 30.7 0.5 CD2 A:LEU144 5.0 17.5 1.0

Zinc binding site 2 out of 2 in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1199 b:32.9 occ:1.00 NE2 B:HIS180 2.0 22.4 1.0 NE2 B:HIS138 2.0 28.6 1.0 OE1 B:GLU142 2.0 29.8 1.0 O B:HOH2253 2.1 22.9 1.0 CD B:GLU142 2.8 22.7 1.0 CD2 B:HIS138 2.8 28.4 1.0 OE2 B:GLU142 2.9 31.1 1.0 CE1 B:HIS180 2.9 22.5 1.0 CD2 B:HIS180 3.1 21.8 1.0 CE1 B:HIS138 3.1 35.6 1.0 CG B:HIS138 4.0 33.3 1.0 ND1 B:HIS180 4.0 25.2 1.0 ND1 B:HIS138 4.1 27.2 1.0 CG B:HIS180 4.1 21.9 1.0 O B:HOH2209 4.2 32.8 1.0 ND2 B:ASN135 4.2 30.4 1.0 CG B:GLU142 4.2 19.9 1.0 O1 B:SO41205 4.5 70.3 1.0 OD1 B:ASN197 4.6 27.1 0.5 CB B:GLU142 4.7 18.9 1.0 ND2 B:ASN197 4.8 31.1 0.5

K.Mcluskey, S.Cameron, F.Hammerschmidt, W.N.Hunter. Structure and Reactivity of Hydroxypropylphosphonic Acid Epoxidase in Fosfomycin Biosynthesis By A Cation- and Flavin- Dependent Mechanism. Proc.Natl.Acad.Sci.Usa V. 102 14221 2005.
ISSN: ISSN 0027-8424
PubMed: 16186494
DOI: 10.1073/PNAS.0504314102