Copper in PDB 3cwy: Structure of Cagd From H. Pylori Pathogenicity Island Crystallized in the Presence of Cu(II) Ions

The structure of Structure of Cagd From H. Pylori Pathogenicity Island Crystallized in the Presence of Cu(II) Ions, PDB code: 3cwy was solved by L.Cendron, G.Zanotti, A.Angelini, N.Barison, M.Couturier, M.Stein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	56.34 / 2.75
Space group	P 62 2 2
Cell size a, b, c (Å), α, β, γ (°)	65.030, 65.030, 156.160, 90.00, 90.00, 120.00
R / Rfree (%)	26.1 / 30.7

The binding sites of Copper atom in the Structure of Cagd From H. Pylori Pathogenicity Island Crystallized in the Presence of Cu(II) Ions (pdb code 3cwy). 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 Structure of Cagd From H. Pylori Pathogenicity Island Crystallized in the Presence of Cu(II) Ions, PDB code: 3cwy:

Copper binding site 1 out of 1 in the Structure of Cagd From H. Pylori Pathogenicity Island Crystallized in the Presence of Cu(II) Ions


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Cagd From H. Pylori Pathogenicity Island Crystallized in the Presence of Cu(II) Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:55.8 occ:1.00 NE2 A:HIS156 2.1 40.6 1.0 O A:HOH303 2.8 2.0 1.0 CD2 A:HIS156 3.0 41.0 1.0 CE1 A:HIS156 3.2 41.4 1.0 CD2 A:TYR148 4.0 41.5 1.0 NE2 A:HIS75 4.2 52.5 1.0 CG A:HIS156 4.2 40.8 1.0 ND1 A:HIS156 4.2 40.3 1.0 O A:ILE99 4.2 43.9 1.0 CE2 A:TYR148 4.4 41.0 1.0 CG2 A:VAL160 4.6 32.0 1.0 CG A:TYR148 4.9 40.7 1.0 CD2 A:HIS75 4.9 53.1 1.0

L.Cendron, M.Couturier, A.Angelini, N.Barison, M.Stein, G.Zanotti. The Helicobacter Pylori Cagd (HP0545, CAG24) Protein Is Essential For Caga Translocation and Maximal Induction of Interleukin-8 Secretion. J.Mol.Biol. V. 386 204 2009.
ISSN: ISSN 0022-2836
PubMed: 19109970
DOI: 10.1016/J.JMB.2008.12.018