Zinc in PDB 2prs: Structure and Metal Binding Properties of Znua, A Periplasmic Zinc Transporter From Escherichia Coli

The structure of Structure and Metal Binding Properties of Znua, A Periplasmic Zinc Transporter From Escherichia Coli, PDB code: 2prs was solved by L.A.Yatsunyk, L.R.Kim, I.I.Vorontsov, A.C.Rosenzweig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.80 / 1.70
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	91.377, 78.073, 86.366, 90.00, 91.37, 90.00
R / Rfree (%)	21.1 / 25

The binding sites of Zinc atom in the Structure and Metal Binding Properties of Znua, A Periplasmic Zinc Transporter From Escherichia Coli (pdb code 2prs). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Structure and Metal Binding Properties of Znua, A Periplasmic Zinc Transporter From Escherichia Coli, PDB code: 2prs:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Structure and Metal Binding Properties of Znua, A Periplasmic Zinc Transporter From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure and Metal Binding Properties of Znua, A Periplasmic Zinc Transporter From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:23.6 occ:1.00 OE1 A:GLU59 2.0 23.9 1.0 NE2 A:HIS60 2.0 23.9 1.0 NE2 A:HIS143 2.0 19.8 1.0 NE2 A:HIS207 2.0 23.0 1.0 CD2 A:HIS60 2.9 23.7 1.0 CD2 A:HIS207 2.9 24.0 1.0 CD2 A:HIS143 3.0 22.1 1.0 CD A:GLU59 3.0 24.5 1.0 CE1 A:HIS60 3.0 26.5 1.0 CE1 A:HIS143 3.0 22.5 1.0 CE1 A:HIS207 3.1 22.5 1.0 CG A:GLU59 3.6 22.9 1.0 OE2 A:GLU59 3.9 25.2 1.0 CG A:HIS60 4.0 24.0 1.0 ND1 A:HIS60 4.1 28.3 1.0 CG A:HIS207 4.1 24.9 1.0 ND1 A:HIS143 4.1 19.8 1.0 CG A:HIS143 4.1 22.0 1.0 ND1 A:HIS207 4.2 24.7 1.0 CB A:ALA209 4.3 24.5 1.0 O A:HOH691 4.3 34.4 1.0 O A:HOH629 4.5 26.9 1.0 CE A:MET85 4.8 28.2 1.0

Zinc binding site 2 out of 3 in the Structure and Metal Binding Properties of Znua, A Periplasmic Zinc Transporter From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure and Metal Binding Properties of Znua, A Periplasmic Zinc Transporter From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn503 b:38.9 occ:0.35 NE2 A:HIS224 2.1 35.0 1.0 CE1 A:HIS224 2.8 34.2 1.0 CD2 A:HIS224 3.3 34.6 1.0 CG2 A:VAL227 3.7 41.9 1.0 ND1 A:HIS224 4.0 34.4 1.0 CG A:HIS224 4.3 34.3 1.0 O A:HOH736 4.3 38.0 1.0 OD2 A:ASP208 4.8 33.6 1.0

Zinc binding site 3 out of 3 in the Structure and Metal Binding Properties of Znua, A Periplasmic Zinc Transporter From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure and Metal Binding Properties of Znua, A Periplasmic Zinc Transporter From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:24.9 occ:1.00 NE2 B:HIS207 2.0 25.4 1.0 NE2 B:HIS60 2.0 22.5 1.0 OE1 B:GLU59 2.0 26.2 1.0 NE2 B:HIS143 2.1 22.4 1.0 CE1 B:HIS207 2.8 25.2 1.0 CD2 B:HIS60 2.9 25.8 1.0 CD2 B:HIS143 3.0 22.0 1.0 CD B:GLU59 3.1 27.8 1.0 CE1 B:HIS60 3.1 26.2 1.0 CE1 B:HIS143 3.1 24.8 1.0 CD2 B:HIS207 3.1 23.8 1.0 CG B:GLU59 3.6 25.4 1.0 O B:HOH649 3.6 47.6 1.0 ND1 B:HIS207 4.0 25.1 1.0 CG B:HIS60 4.1 25.0 1.0 ND1 B:HIS60 4.1 26.6 1.0 OE2 B:GLU59 4.1 27.2 1.0 CG B:HIS207 4.2 25.1 1.0 ND1 B:HIS143 4.2 21.3 1.0 CG B:HIS143 4.2 21.8 1.0 O B:HOH650 4.5 34.7 1.0 CB B:ALA209 4.5 22.8 1.0 O B:HOH526 4.8 29.9 1.0 CE B:MET85 4.8 26.5 1.0 O B:HOH708 4.8 40.6 1.0 O B:HOH647 4.9 41.2 1.0

L.A.Yatsunyk, J.A.Easton, L.R.Kim, S.A.Sugarbaker, B.Bennett, R.M.Breece, I.I.Vorontsov, D.L.Tierney, M.W.Crowder, A.C.Rosenzweig. Structure and Metal Binding Properties of Znua, A Periplasmic Zinc Transporter From Escherichia Coli. J.Biol.Inorg.Chem. V. 13 271 2008.
ISSN: ISSN 0949-8257
PubMed: 18027003
DOI: 10.1007/S00775-007-0320-0