Zinc in PDB 3p3g: Crystal Structure of the Escherichia Coli Lpxc/Lpc-009 Complex

Protein crystallography data

The structure of Crystal Structure of the Escherichia Coli Lpxc/Lpc-009 Complex, PDB code: 3p3g was solved by C.-J.Lee, P.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.60 / 1.65
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 106.725, 106.725, 52.684, 90.00, 90.00, 120.00
R / Rfree (%) 15.5 / 17.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Escherichia Coli Lpxc/Lpc-009 Complex (pdb code 3p3g). 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 Crystal Structure of the Escherichia Coli Lpxc/Lpc-009 Complex, PDB code: 3p3g:

Zinc binding site 1 out of 1 in 3p3g

Go back to Zinc Binding Sites List in 3p3g
Zinc binding site 1 out of 1 in the Crystal Structure of the Escherichia Coli Lpxc/Lpc-009 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Escherichia Coli Lpxc/Lpc-009 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:18.8
occ:1.00
O01 A:3P3401 2.0 20.7 1.0
OD1 A:ASP242 2.1 19.6 1.0
NE2 A:HIS79 2.1 16.9 1.0
NE2 A:HIS238 2.1 20.9 1.0
O04 A:3P3401 2.1 20.3 1.0
OD2 A:ASP242 2.4 23.7 1.0
CG A:ASP242 2.6 20.9 1.0
C02 A:3P3401 2.8 21.1 1.0
N03 A:3P3401 2.9 21.0 1.0
CE1 A:HIS238 3.0 17.9 1.0
CD2 A:HIS79 3.1 16.1 1.0
CE1 A:HIS79 3.1 16.1 1.0
CD2 A:HIS238 3.1 18.4 1.0
HE1 A:HIS238 3.2 21.6 1.0
HD2 A:HIS79 3.2 19.3 1.0
HE1 A:HIS79 3.3 19.3 1.0
HD2 A:HIS238 3.3 22.1 1.0
HG1 A:THR191 3.6 26.7 1.0
HB A:THR191 3.6 24.0 1.0
HG3 A:GLU78 4.0 25.1 1.0
CB A:ASP242 4.1 20.5 1.0
HE1 A:HIS265 4.1 27.7 1.0
OG1 A:THR191 4.1 22.3 1.0
ND1 A:HIS238 4.1 18.8 1.0
HG2 A:GLU78 4.2 25.1 1.0
ND1 A:HIS79 4.2 16.1 1.0
CG A:HIS238 4.2 19.0 1.0
CG A:HIS79 4.2 17.3 1.0
OE2 A:GLU78 4.2 28.5 1.0
C05 A:3P3401 4.2 23.3 1.0
HZ2 A:LYS239 4.3 37.8 1.0
CB A:THR191 4.3 20.0 1.0
HA A:ASP242 4.5 25.5 1.0
HA A:THR191 4.5 20.5 1.0
HB3 A:ASP242 4.5 24.6 1.0
CG A:GLU78 4.5 20.9 1.0
HB2 A:ASP242 4.5 24.6 1.0
HD23 A:LEU241 4.7 23.3 1.0
CE1 A:HIS265 4.7 23.1 1.0
CA A:ASP242 4.8 21.2 1.0
NE2 A:HIS265 4.8 23.1 1.0
C26 A:3P3401 4.8 28.3 1.0
N06 A:3P3401 4.8 23.6 1.0
HZ3 A:LYS239 4.8 37.8 1.0
O A:HIS238 4.9 20.7 1.0
H A:ASP242 4.9 24.7 1.0
CD A:GLU78 4.9 35.7 1.0
HD1 A:HIS238 4.9 22.5 1.0
O27 A:3P3401 4.9 29.1 1.0
CA A:THR191 4.9 17.1 1.0
C25 A:3P3401 4.9 26.6 1.0
HD1 A:HIS79 5.0 19.4 1.0

Reference:

C.J.Lee, X.Liang, X.Chen, D.Zeng, S.H.Joo, H.S.Chung, A.W.Barb, S.M.Swanson, R.A.Nicholas, Y.Li, E.J.Toone, C.R.Raetz, P.Zhou. Species-Specific and Inhibitor-Dependent Conformations of Lpxc: Implications For Antibiotic Design. Chem.Biol. V. 18 38 2011.
ISSN: ISSN 1074-5521
PubMed: 21167751
DOI: 10.1016/J.CHEMBIOL.2010.11.011
Page generated: Wed Dec 16 04:42:21 2020

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