Copper in PDB 3cvb: Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization

The structure of Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization, PDB code: 3cvb was solved by P.B.Crowley, P.M.Matias, H.Mi, S.J.Firbank, M.J.Banfield, C.Dennison, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.89 / 1.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	33.735, 33.415, 78.471, 90.00, 90.55, 90.00
R / Rfree (%)	13.8 / 18.3

The binding sites of Copper atom in the Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization (pdb code 3cvb). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization, PDB code: 3cvb:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu106 b:8.3 occ:1.00 ND1 A:HIS39 2.1 5.5 1.0 SG A:CYS89 2.2 5.0 1.0 ND1 A:HIS92 2.3 3.5 0.5 SD A:MET97 2.5 4.8 1.0 CD2 A:HIS92 2.9 7.2 0.5 CE1 A:HIS39 3.0 6.2 1.0 CG A:HIS39 3.1 5.5 1.0 CB A:CYS89 3.2 4.6 1.0 CE1 A:HIS92 3.2 6.7 0.5 CE A:MET97 3.3 7.0 1.0 CG A:HIS92 3.3 4.6 0.5 CB A:HIS39 3.5 6.1 1.0 CG A:HIS92 3.6 5.6 0.5 CB A:HIS92 3.6 4.9 0.5 CB A:HIS92 3.7 5.3 0.5 CG A:MET97 3.8 5.1 1.0 CA A:HIS39 3.8 4.8 1.0 NE2 A:HIS92 4.0 8.9 0.5 NE2 A:HIS39 4.1 6.0 1.0 CD2 A:HIS39 4.2 5.3 1.0 O A:PRO38 4.3 6.0 1.0 NE2 A:HIS92 4.3 7.7 0.5 N A:HIS92 4.4 4.7 1.0 CB A:MET97 4.4 4.9 1.0 CD2 A:HIS92 4.4 8.5 0.5 CA A:CYS89 4.6 3.9 1.0 CA A:HIS92 4.6 4.8 0.5 CA A:HIS92 4.6 4.9 0.5 CB A:PRO91 4.7 5.6 1.0 N A:HIS39 4.8 4.3 1.0 N A:ASN40 4.8 4.7 1.0 ND1 A:HIS92 4.9 7.4 0.5 C A:HIS39 4.9 4.2 1.0 C A:PRO38 4.9 5.5 1.0

Copper binding site 2 out of 2 in the Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu106 b:8.9 occ:1.00 ND1 B:HIS39 2.1 5.3 1.0 SG B:CYS89 2.2 5.8 1.0 ND1 B:HIS92 2.3 5.2 0.5 SD B:MET97 2.5 5.9 1.0 CE1 B:HIS39 3.0 5.7 1.0 CG B:HIS39 3.1 5.3 1.0 CD2 B:HIS92 3.1 9.9 0.5 CB B:CYS89 3.2 5.3 1.0 CE1 B:HIS92 3.2 6.5 0.5 CE B:MET97 3.2 8.4 1.0 CG B:HIS92 3.3 5.9 0.5 CB B:HIS39 3.4 5.8 1.0 CB B:HIS92 3.6 6.6 0.5 CG B:HIS92 3.8 7.9 0.5 CA B:HIS39 3.8 5.4 1.0 CB B:HIS92 3.8 7.4 0.5 CG B:MET97 3.8 5.6 1.0 NE2 B:HIS39 4.1 5.8 1.0 CD2 B:HIS39 4.2 6.0 1.0 O B:PRO38 4.3 6.2 1.0 NE2 B:HIS92 4.3 9.2 0.5 NE2 B:HIS92 4.3 8.4 0.5 N B:HIS92 4.4 6.3 1.0 CB B:MET97 4.4 6.2 1.0 CD2 B:HIS92 4.4 8.8 0.5 CA B:CYS89 4.6 4.8 1.0 CA B:HIS92 4.6 7.0 0.5 CB B:PRO91 4.7 8.2 1.0 CA B:HIS92 4.7 7.2 0.5 N B:HIS39 4.8 5.3 1.0 N B:ASN40 4.8 5.0 1.0 C B:HIS39 4.9 5.5 1.0 C B:PRO38 4.9 5.7 1.0

P.B.Crowley, P.M.Matias, H.Mi, S.J.Firbank, M.J.Banfield, C.Dennison. Regulation of Protein Function: Crystal Packing Interfaces and Conformational Dimerization. Biochemistry V. 47 6583 2008.
ISSN: ISSN 0006-2960
PubMed: 18479147
DOI: 10.1021/BI800125H