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Copper in PDB 3e6z: 1.0 A Structure of Cusf-W44A-Cu(II) Residues 10-88 From Escherichia Coli

Protein crystallography data

The structure of 1.0 A Structure of Cusf-W44A-Cu(II) Residues 10-88 From Escherichia Coli, PDB code: 3e6z was solved by I.R.Loftin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.33 / 1.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 26.272, 31.615, 84.685, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 21.4

Copper Binding Sites:

The binding sites of Copper atom in the 1.0 A Structure of Cusf-W44A-Cu(II) Residues 10-88 From Escherichia Coli (pdb code 3e6z). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the 1.0 A Structure of Cusf-W44A-Cu(II) Residues 10-88 From Escherichia Coli, PDB code: 3e6z:

Copper binding site 1 out of 1 in 3e6z

Go back to Copper Binding Sites List in 3e6z
Copper binding site 1 out of 1 in the 1.0 A Structure of Cusf-W44A-Cu(II) Residues 10-88 From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of 1.0 A Structure of Cusf-W44A-Cu(II) Residues 10-88 From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Cu1

b:12.5
occ:0.70
NE2 X:HIS36 2.0 11.9 1.0
CE X:MET47 2.1 16.2 0.3
SD X:MET47 2.3 12.8 0.7
SD X:MET49 2.3 12.2 0.7
CE1 X:HIS36 2.9 11.6 1.0
CD2 X:HIS36 3.1 11.4 1.0
CE X:MET47 3.3 14.1 0.7
CG X:MET47 3.3 12.2 0.7
CB X:MET47 3.4 12.0 0.7
CE X:MET49 3.4 12.3 0.7
CG X:MET49 3.4 10.8 0.7
SD X:MET47 3.7 16.2 0.3
CB X:MET47 3.8 13.8 0.3
CG X:MET49 3.8 13.5 0.3
ND1 X:HIS36 4.1 11.7 1.0
CG X:MET47 4.2 14.4 0.3
CG X:HIS36 4.2 10.8 1.0
CB X:ALA44 4.5 13.6 1.0
CB X:MET49 4.8 10.6 0.7
SD X:MET49 4.8 15.6 0.3
CA X:MET47 4.8 12.0 0.7
CB X:MET49 4.8 12.7 0.3
CD1 X:ILE39 4.9 12.7 1.0
CA X:MET47 4.9 13.2 0.3
O X:PRO45 4.9 13.0 1.0

Reference:

I.R.Loftin, N.J.Blackburn, M.M.Mcevoy. Tryptophan Cu(I)-Pi Interaction Fine-Tunes the Metal Binding Properties of the Bacterial Metallochaperone Cusf J.Biol.Inorg.Chem. V. 14 905 2009.
ISSN: ISSN 0949-8257
PubMed: 19381697
DOI: 10.1007/S00775-009-0503-Y
Page generated: Thu Sep 3 17:11:39 2020
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