Copper in PDB 2fqg: Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations

The structure of Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations, PDB code: 2fqg was solved by X.Li, Z.Wei, M.Zhang, M.Teng, W.Gong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.30
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	69.114, 73.036, 189.437, 90.00, 90.00, 90.00
R / Rfree (%)	15.7 / 23.3

The structure of Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Copper atom in the Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations (pdb code 2fqg). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations, PDB code: 2fqg:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu601 b:23.9 occ:1.00 ND1 A:HIS443 2.0 21.8 1.0 ND1 A:HIS505 2.2 24.4 1.0 SG A:CYS500 2.2 21.5 1.0 CE1 A:HIS443 3.0 23.5 1.0 CG A:HIS443 3.1 19.9 1.0 CG A:HIS505 3.1 23.4 1.0 CE1 A:HIS505 3.1 25.8 1.0 CB A:CYS500 3.2 14.8 1.0 SD A:MET510 3.3 19.4 1.0 CB A:HIS505 3.4 21.0 1.0 CB A:HIS443 3.4 21.4 1.0 CA A:HIS443 3.7 19.4 1.0 O A:LEU442 3.7 24.6 1.0 CE A:MET510 4.0 16.9 1.0 CB A:LEU502 4.1 16.0 1.0 NE2 A:HIS443 4.1 24.7 1.0 CD2 A:HIS443 4.2 21.2 1.0 NE2 A:HIS505 4.2 25.2 1.0 CD2 A:HIS505 4.2 25.4 1.0 C A:LEU442 4.4 23.5 1.0 N A:HIS443 4.5 20.2 1.0 CA A:CYS500 4.6 17.9 1.0 CD1 A:LEU502 4.7 21.1 1.0 CG A:MET510 4.9 17.0 1.0 O A:LEU502 4.9 16.4 1.0 C A:HIS443 4.9 19.2 1.0 CG A:LEU502 4.9 24.2 1.0 CA A:HIS505 4.9 21.1 1.0 N A:LEU502 4.9 18.5 1.0

Copper binding site 2 out of 4 in the Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu603 b:31.0 occ:0.50 NE2 A:HIS101 2.0 24.0 1.0 NE2 A:HIS446 2.1 17.8 1.0 O A:HOH983 2.7 22.8 1.0 CE1 A:HIS101 2.8 19.9 1.0 CD2 A:HIS446 2.9 16.1 1.0 CD2 A:HIS101 3.1 22.9 1.0 CD2 A:HIS448 3.1 18.1 1.0 NE2 A:HIS448 3.1 22.1 1.0 O1 A:C2O602 3.1 25.5 0.8 CE1 A:HIS446 3.1 21.2 1.0 CG A:HIS103 3.5 14.3 1.0 CU2 A:C2O602 3.5 24.7 0.6 CA A:HIS103 3.5 19.0 1.0 ND1 A:HIS103 3.6 18.2 1.0 CB A:HIS103 3.6 15.7 1.0 CE1 A:HIS448 3.7 21.7 1.0 CG A:HIS448 3.7 21.4 1.0 CU3 A:C2O602 3.9 25.5 0.8 CD2 A:HIS103 4.0 13.9 1.0 ND1 A:HIS101 4.0 23.2 1.0 ND1 A:HIS448 4.1 23.0 1.0 CG A:HIS446 4.1 19.2 1.0 CE1 A:HIS103 4.2 14.2 1.0 CG A:HIS101 4.2 20.7 1.0 ND1 A:HIS446 4.2 20.1 1.0 N A:GLY104 4.2 15.3 1.0 NE2 A:HIS103 4.4 13.3 1.0 C A:HIS103 4.4 18.4 1.0 N A:HIS103 4.6 20.1 1.0 CA A:HIS448 4.6 18.5 1.0 O A:HOH1015 4.6 28.0 1.0 O A:HOH994 4.7 25.8 1.0 CB A:HIS448 4.7 18.7 1.0 O A:TRP102 4.8 19.7 1.0 NE2 A:HIS499 5.0 18.5 1.0 C A:TRP102 5.0 20.3 1.0

Copper binding site 3 out of 4 in the Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu602 b:24.7 occ:0.60 CU2 A:C2O602 0.0 24.7 0.6 O1 A:C2O602 2.0 25.5 0.8 NE2 A:HIS448 2.1 22.1 1.0 NE2 A:HIS499 2.1 18.5 1.0 NE2 A:HIS143 2.2 30.1 1.0 CE1 A:HIS448 2.9 21.7 1.0 O A:HOH1137 3.0 49.9 1.0 CE1 A:HIS499 3.0 16.1 1.0 CD2 A:HIS499 3.1 18.2 1.0 CD2 A:HIS143 3.1 27.5 1.0 CD2 A:HIS448 3.2 18.1 1.0 CE1 A:HIS143 3.2 28.8 1.0 CU A:CU603 3.5 31.0 0.5 NE2 A:HIS101 3.6 24.0 1.0 CD2 A:HIS446 3.6 16.1 1.0 CD2 A:HIS101 3.7 22.9 1.0 CU3 A:C2O602 4.0 25.5 0.8 ND1 A:HIS448 4.1 23.0 1.0 ND1 A:HIS499 4.1 16.5 1.0 NE2 A:HIS446 4.1 17.8 1.0 CG A:HIS499 4.2 18.9 1.0 CG A:HIS448 4.2 21.4 1.0 CG A:HIS143 4.3 26.5 1.0 ND1 A:HIS143 4.3 29.0 1.0 CE1 A:HIS101 4.5 19.9 1.0 CG A:HIS101 4.6 20.7 1.0 CE1 A:HIS141 4.7 18.3 1.0 CD2 A:HIS501 4.7 16.7 1.0 NE2 A:HIS501 4.7 19.4 1.0 CG A:HIS446 4.8 19.2 1.0 NE2 A:HIS141 4.9 21.6 1.0 CB A:MET497 4.9 22.2 1.0 OE1 A:GLU506 5.0 28.6 1.0

Copper binding site 4 out of 4 in the Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structures of E. Coli Laccase Cueo Under Different Copper Binding Situations within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu602 b:25.5 occ:0.80 CU3 A:C2O602 0.0 25.5 0.8 ND1 A:HIS103 1.9 18.2 1.0 O1 A:C2O602 2.0 25.5 0.8 NE2 A:HIS141 2.1 21.6 1.0 NE2 A:HIS501 2.2 19.4 1.0 CE1 A:HIS103 2.9 14.2 1.0 CG A:HIS103 3.0 14.3 1.0 CE1 A:HIS141 3.0 18.3 1.0 CD2 A:HIS501 3.1 16.7 1.0 CD2 A:HIS141 3.2 19.1 1.0 CE1 A:HIS501 3.2 19.3 1.0 CB A:HIS103 3.4 15.7 1.0 O A:HOH1137 3.9 49.9 1.0 CU A:CU603 3.9 31.0 0.5 CZ2 A:TRP139 4.0 12.7 1.0 NE2 A:HIS103 4.0 13.3 1.0 CD2 A:HIS101 4.0 22.9 1.0 CU2 A:C2O602 4.0 24.7 0.6 CD2 A:HIS103 4.1 13.9 1.0 ND1 A:HIS141 4.2 17.9 1.0 CG A:HIS141 4.3 20.0 1.0 CG A:HIS501 4.3 17.7 1.0 ND1 A:HIS501 4.3 18.1 1.0 NE2 A:HIS101 4.3 24.0 1.0 CE2 A:TRP139 4.3 11.1 1.0 CD2 A:HIS446 4.4 16.1 1.0 NE1 A:TRP139 4.5 12.6 1.0 NE2 A:HIS446 4.5 17.8 1.0 CH2 A:TRP139 4.6 14.6 1.0 CA A:HIS103 4.7 19.0 1.0

X.Li, Z.Wei, M.Zhang, X.Peng, G.Yu, M.Teng, W.Gong. Crystal Structures of E. Coli Laccase Cueo at Different Copper Concentrations. Biochem.Biophys.Res.Commun. V. 354 21 2007.
ISSN: ISSN 0006-291X
PubMed: 17217912
DOI: 10.1016/J.BBRC.2006.12.116