Zinc in PDB 4f6z: Mutagenesis of Zinc Ligand Residue CYS221 Reveals Plasticity in the Imp-1 Metallo-B-Lactamase Active Site

The structure of Mutagenesis of Zinc Ligand Residue CYS221 Reveals Plasticity in the Imp-1 Metallo-B-Lactamase Active Site, PDB code: 4f6z was solved by L.B.Horton, S.Shanker, R.Mikulski, N.G.Brown, K.Phillips, E.Lykissa, B.V.V.Prasad, T.G.Palzkill, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.24 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.031, 59.774, 83.552, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 24.9

The binding sites of Zinc atom in the Mutagenesis of Zinc Ligand Residue CYS221 Reveals Plasticity in the Imp-1 Metallo-B-Lactamase Active Site (pdb code 4f6z). 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 Mutagenesis of Zinc Ligand Residue CYS221 Reveals Plasticity in the Imp-1 Metallo-B-Lactamase Active Site, PDB code: 4f6z:

Zinc binding site 1 out of 1 in the Mutagenesis of Zinc Ligand Residue CYS221 Reveals Plasticity in the Imp-1 Metallo-B-Lactamase Active Site


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mutagenesis of Zinc Ligand Residue CYS221 Reveals Plasticity in the Imp-1 Metallo-B-Lactamase Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:28.4 occ:1.00 ND1 A:HIS79 2.0 23.4 1.0 NE2 A:HIS77 2.1 20.1 1.0 NE2 A:HIS139 2.2 24.5 1.0 CG A:FLC302 2.3 34.7 1.0 CE1 A:HIS79 3.0 21.5 1.0 CD2 A:HIS77 3.0 17.4 1.0 CG A:HIS79 3.0 20.0 1.0 CD2 A:HIS139 3.0 24.0 1.0 CA A:FLC302 3.1 27.3 1.0 CB A:FLC302 3.1 18.1 1.0 CE1 A:HIS77 3.2 24.1 1.0 CE1 A:HIS139 3.2 24.7 1.0 CB A:HIS79 3.4 23.8 1.0 CGC A:FLC302 3.5 52.0 1.0 OHB A:FLC302 3.6 34.2 1.0 CAC A:FLC302 3.6 64.5 1.0 OG2 A:FLC302 3.6 38.3 1.0 OA2 A:FLC302 3.7 74.3 1.0 OD1 A:ASP81 3.9 31.3 1.0 NE2 A:HIS79 4.1 25.9 1.0 CD2 A:HIS79 4.1 24.4 1.0 CG A:HIS77 4.2 23.2 1.0 CG A:HIS139 4.2 24.6 1.0 ND1 A:HIS77 4.2 26.7 1.0 ND1 A:HIS139 4.3 23.4 1.0 OA1 A:FLC302 4.4 48.3 1.0 CBC A:FLC302 4.4 35.4 1.0 CG2 A:THR140 4.4 25.5 1.0 OG1 A:FLC302 4.6 66.3 1.0 OB2 A:FLC302 4.7 48.8 1.0 CG A:ASP81 4.7 29.0 1.0 CA A:HIS79 4.8 24.8 1.0 OD2 A:ASP81 4.8 43.9 1.0

L.B.Horton, S.Shanker, R.Mikulski, N.G.Brown, K.J.Phillips, E.Lykissa, B.V.Venkataram Prasad, T.Palzkill. Mutagenesis of Zinc Ligand Residue CYS221 Reveals Plasticity in the Imp-1 Metallo-Beta-Lactamase Active Site Antimicrob.Agents Chemother. V. 56 5667 2012.
ISSN: ISSN 0066-4804
PubMed: 22908171
DOI: 10.1128/AAC.01276-12