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Zinc in PDB 4f6h: Mutagenesis of Zinc Ligand Residue CYS221 Reveals Plasticity in the Imp-1 Metallo-B-Lactamase Active Site

Protein crystallography data

The structure of Mutagenesis of Zinc Ligand Residue CYS221 Reveals Plasticity in the Imp-1 Metallo-B-Lactamase Active Site, PDB code: 4f6h 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) 30.25 / 1.74
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.016, 60.499, 84.287, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 22.6

Zinc Binding Sites:

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 4f6h). 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: 4f6h:

Zinc binding site 1 out of 1 in 4f6h

Go back to Zinc Binding Sites List in 4f6h
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:19.2
occ:0.68
O3 A:SO4304 2.0 21.7 0.8
ND1 A:HIS79 2.0 23.5 1.0
NE2 A:HIS77 2.1 20.1 1.0
NE2 A:HIS139 2.2 25.6 1.0
S A:SO4304 2.9 47.6 0.8
CD2 A:HIS77 2.9 20.4 1.0
CE1 A:HIS79 2.9 21.1 1.0
CG A:HIS79 3.0 15.2 1.0
CD2 A:HIS139 3.1 24.5 1.0
O2 A:SO4304 3.2 45.0 0.8
CE1 A:HIS77 3.2 22.0 1.0
CE1 A:HIS139 3.2 28.2 1.0
O4 A:SO4304 3.3 34.5 0.8
CB A:HIS79 3.4 14.5 1.0
NE2 A:HIS79 4.1 22.1 1.0
CG A:HIS77 4.1 18.0 1.0
OD1 A:ASP81 4.1 36.2 1.0
CD2 A:HIS79 4.1 22.6 1.0
O1 A:SO4304 4.2 52.0 0.8
ND1 A:HIS77 4.2 22.5 1.0
CG A:HIS139 4.3 24.0 1.0
ND1 A:HIS139 4.3 24.2 1.0
CG2 A:THR140 4.4 21.6 1.0
OD2 A:ASP81 4.8 44.4 1.0
CA A:HIS79 4.9 15.1 1.0
CG A:ASP81 4.9 29.7 1.0

Reference:

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
Page generated: Wed Dec 16 05:17:01 2020

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