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Zinc in PDB 4uwr: Mono-Zinc Vim-26. LEU224 in Vim-26 From Klebsiella Pneumoniae Has Implications For Drug Binding.

Protein crystallography data

The structure of Mono-Zinc Vim-26. LEU224 in Vim-26 From Klebsiella Pneumoniae Has Implications For Drug Binding., PDB code: 4uwr was solved by H.-K.S.Leiros, K.S.W.Edvardsen, G.E.K.Bjerga, O.Samuelsen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.070 / 1.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.735, 67.783, 40.408, 90.00, 93.07, 90.00
R / Rfree (%) 15.38 / 18.22

Other elements in 4uwr:

The structure of Mono-Zinc Vim-26. LEU224 in Vim-26 From Klebsiella Pneumoniae Has Implications For Drug Binding. also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Mono-Zinc Vim-26. LEU224 in Vim-26 From Klebsiella Pneumoniae Has Implications For Drug Binding. (pdb code 4uwr). 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 Mono-Zinc Vim-26. LEU224 in Vim-26 From Klebsiella Pneumoniae Has Implications For Drug Binding., PDB code: 4uwr:

Zinc binding site 1 out of 1 in 4uwr

Go back to Zinc Binding Sites List in 4uwr
Zinc binding site 1 out of 1 in the Mono-Zinc Vim-26. LEU224 in Vim-26 From Klebsiella Pneumoniae Has Implications For Drug Binding.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mono-Zinc Vim-26. LEU224 in Vim-26 From Klebsiella Pneumoniae Has Implications For Drug Binding. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1297

b:16.0
occ:1.00
O B:HOH2067 1.9 19.4 1.0
ND1 B:HIS118 2.0 16.8 1.0
NE2 B:HIS196 2.0 11.9 1.0
NE2 B:HIS116 2.1 13.6 1.0
O B:HOH2068 2.6 26.6 1.0
CE1 B:HIS118 2.9 16.2 1.0
HB2 B:HIS118 2.9 18.1 1.0
CE1 B:HIS116 3.0 11.0 1.0
CD2 B:HIS196 3.0 13.4 1.0
CE1 B:HIS196 3.0 16.9 1.0
CG B:HIS118 3.1 16.3 1.0
HE1 B:HIS118 3.1 19.4 1.0
HE1 B:HIS116 3.1 13.2 1.0
CD2 B:HIS116 3.2 12.6 1.0
HD2 B:HIS196 3.2 16.1 1.0
HE1 B:HIS196 3.2 20.3 1.0
HD2 B:HIS116 3.4 15.1 1.0
CB B:HIS118 3.4 15.1 1.0
HB3 B:HIS118 3.7 18.1 1.0
OD2 B:OCS221 3.8 17.8 1.0
OD1 B:ASP120 3.9 20.8 1.0
NE2 B:HIS118 4.1 21.3 1.0
ND1 B:HIS116 4.1 12.7 1.0
ND1 B:HIS196 4.1 16.3 1.0
CG B:HIS196 4.1 13.7 1.0
CD2 B:HIS118 4.1 19.5 1.0
HB2 B:OCS221 4.2 15.9 1.0
CG B:HIS116 4.2 14.8 1.0
O B:HOH2071 4.3 47.5 1.0
HD21 B:ASN233 4.4 51.0 1.0
OD1 B:OCS221 4.4 15.9 1.0
H B:HIS118 4.5 18.6 1.0
SG B:OCS221 4.5 15.0 1.0
OD2 B:ASP120 4.7 24.7 1.0
CB B:OCS221 4.7 13.3 1.0
HB3 B:SER197 4.7 17.9 1.0
CG B:ASP120 4.7 18.7 1.0
HB3 B:OCS221 4.7 15.9 1.0
HG2 B:ARG121 4.8 15.8 1.0
CA B:HIS118 4.8 18.3 1.0

Reference:

H.S.Leiros, K.S.W.Edvardsen, G.E.K.Bjerga, O.Samuelsen. Structural and Biochemical Characterization of Vim-26 Show That LEU224 Has Implications For the Substrate Specificity of Vim Metallo-Beta-Lactamases. Febs J. 2015.
ISSN: ESSN 1742-4658
PubMed: 25601024
DOI: 10.1111/FEBS.13200
Page generated: Wed Dec 16 05:49:36 2020

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