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Zinc in PDB 3lnn: Crystal Structure of Zneb From Cupriavidus Metallidurans

Protein crystallography data

The structure of Crystal Structure of Zneb From Cupriavidus Metallidurans, PDB code: 3lnn was solved by J.K.Lee, F.De Angelis, L.J.Miercke, R.M.Stroud, G.Vandenbussche, Centerfor Structures Of Membrane Proteins (Csmp), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.96 / 2.80
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 137.111, 137.111, 202.898, 90.00, 90.00, 90.00
R / Rfree (%) 23.7 / 31.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Zneb From Cupriavidus Metallidurans (pdb code 3lnn). 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 Zneb From Cupriavidus Metallidurans, PDB code: 3lnn:

Zinc binding site 1 out of 1 in 3lnn

Go back to Zinc Binding Sites List in 3lnn
Zinc binding site 1 out of 1 in the Crystal Structure of Zneb From Cupriavidus Metallidurans


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 Zneb From Cupriavidus Metallidurans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn360

b:77.7
occ:1.00
O A:HOH361 2.1 43.6 1.0
NE2 A:HIS221 2.2 67.8 1.0
OE2 A:GLU329 2.3 81.5 1.0
NE2 A:HIS285 2.4 81.7 1.0
OE1 A:GLU329 2.9 83.1 1.0
CD A:GLU329 2.9 81.7 1.0
CD2 A:HIS221 3.0 67.2 1.0
CD2 A:HIS285 3.1 74.6 1.0
CE1 A:HIS221 3.3 77.8 1.0
CE1 A:HIS285 3.5 84.7 1.0
CG2 A:VAL40 4.1 95.8 1.0
CG A:HIS221 4.2 72.5 1.0
ND1 A:HIS221 4.3 76.4 1.0
CG A:HIS285 4.3 73.1 1.0
CG A:GLU329 4.4 72.0 1.0
ND1 A:HIS285 4.4 77.8 1.0

Reference:

F.De Angelis, J.K.Lee, J.D.O'connell, L.J.Miercke, K.H.Verschueren, V.Srinivasan, C.Bauvois, C.Govaerts, R.A.Robbins, J.M.Ruysschaert, R.M.Stroud, G.Vandenbussche. Metal-Induced Conformational Changes in Zneb Suggest An Active Role of Membrane Fusion Proteins in Efflux Resistance Systems. Proc.Natl.Acad.Sci.Usa V. 107 11038 2010.
ISSN: ISSN 0027-8424
PubMed: 20534468
DOI: 10.1073/PNAS.1003908107
Page generated: Wed Dec 16 04:32:40 2020

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