Copper in PDB 1kv7: Crystal Structure of Cueo, A Multi-Copper Oxidase From E. Coli Involved in Copper Homeostasis

The structure of Crystal Structure of Cueo, A Multi-Copper Oxidase From E. Coli Involved in Copper Homeostasis, PDB code: 1kv7 was solved by S.A.Roberts, A.Weichsel, G.Grass, K.Thakali, J.T.Hazzard, G.Tollin, C.Rensing, W.R.Montfort, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.00 / 1.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.820, 90.510, 53.090, 90.00, 102.90, 90.00
R / Rfree (%)	18.5 / 22.1

The binding sites of Copper atom in the Crystal Structure of Cueo, A Multi-Copper Oxidase From E. Coli Involved in Copper Homeostasis (pdb code 1kv7). 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 Structure of Cueo, A Multi-Copper Oxidase From E. Coli Involved in Copper Homeostasis, PDB code: 1kv7:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Crystal Structure of Cueo, A Multi-Copper Oxidase From E. Coli Involved in Copper Homeostasis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Cueo, A Multi-Copper Oxidase From E. Coli Involved in Copper Homeostasis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu701 b:10.7 occ:1.00 ND1 A:HIS505 2.0 11.6 1.0 ND1 A:HIS443 2.0 11.4 1.0 SG A:CYS500 2.2 11.7 1.0 CE1 A:HIS443 3.0 11.2 1.0 CE1 A:HIS505 3.0 12.6 1.0 CG A:HIS505 3.0 9.3 1.0 CG A:HIS443 3.1 9.5 1.0 CB A:CYS500 3.2 10.8 1.0 SD A:MET510 3.2 13.1 1.0 CB A:HIS505 3.3 9.6 1.0 CB A:HIS443 3.5 12.0 1.0 CA A:HIS443 3.7 11.3 1.0 O A:LEU442 3.7 14.5 1.0 CE A:MET510 4.1 12.4 1.0 CB A:LEU502 4.1 9.6 1.0 NE2 A:HIS505 4.1 11.9 1.0 NE2 A:HIS443 4.1 10.3 1.0 CD2 A:HIS505 4.2 12.1 1.0 CD2 A:HIS443 4.2 11.3 1.0 C A:LEU442 4.4 10.4 1.0 N A:HIS443 4.4 9.1 1.0 CA A:CYS500 4.6 12.0 1.0 CD1 A:LEU502 4.7 10.8 1.0 CG A:MET510 4.7 11.7 1.0 CA A:HIS505 4.8 10.7 1.0 C A:HIS443 4.9 10.6 1.0 CG A:LEU502 4.9 11.0 1.0 N A:LEU502 4.9 8.7 1.0 O A:LEU502 4.9 10.6 1.0

Copper binding site 2 out of 4 in the Crystal Structure of Cueo, A Multi-Copper Oxidase From E. Coli Involved in Copper Homeostasis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Cueo, A Multi-Copper Oxidase From E. Coli Involved in Copper Homeostasis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu703 b:30.4 occ:1.00 NE2 A:HIS446 1.8 11.6 1.0 NE2 A:HIS101 1.9 13.9 1.0 CD2 A:HIS446 2.7 11.8 1.0 CE1 A:HIS101 2.8 18.9 1.0 CD2 A:HIS101 2.9 13.7 1.0 CE1 A:HIS446 2.9 12.3 1.0 O A:HOH2018 3.0 15.8 1.0 O1 A:C2O702 3.1 14.2 1.0 CD2 A:HIS448 3.2 13.6 1.0 NE2 A:HIS448 3.2 11.7 1.0 ND1 A:HIS103 3.5 10.7 1.0 CG A:HIS103 3.5 8.4 1.0 CU2 A:C2O702 3.5 22.5 1.0 CA A:HIS103 3.7 10.6 1.0 CB A:HIS103 3.8 9.1 1.0 CG A:HIS448 3.9 12.2 1.0 CG A:HIS446 3.9 12.8 1.0 CE1 A:HIS448 3.9 17.4 1.0 ND1 A:HIS101 3.9 13.5 1.0 ND1 A:HIS446 4.0 14.7 1.0 CU3 A:C2O702 4.0 14.8 1.0 CG A:HIS101 4.0 11.4 1.0 CE1 A:HIS103 4.0 7.7 1.0 CD2 A:HIS103 4.1 9.3 1.0 ND1 A:HIS448 4.2 15.0 1.0 NE2 A:HIS103 4.4 10.4 1.0 N A:GLY104 4.5 9.8 1.0 N A:HIS103 4.6 10.6 1.0 C A:HIS103 4.6 9.8 1.0 CA A:HIS448 4.7 10.5 1.0 CB A:HIS448 4.8 10.9 1.0 NE2 A:HIS499 4.8 11.7 1.0 O A:TRP102 4.9 10.5 1.0 NE2 A:HIS141 5.0 12.9 1.0 O A:HOH2058 5.0 16.6 1.0

Copper binding site 3 out of 4 in the Crystal Structure of Cueo, A Multi-Copper Oxidase From E. Coli Involved in Copper Homeostasis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Cueo, A Multi-Copper Oxidase From E. Coli Involved in Copper Homeostasis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu702 b:22.5 occ:1.00 CU2 A:C2O702 0.0 22.5 1.0 NE2 A:HIS448 1.9 11.7 1.0 NE2 A:HIS143 2.0 18.2 1.0 NE2 A:HIS499 2.0 11.7 1.0 O1 A:C2O702 2.3 14.2 1.0 CE1 A:HIS448 2.8 17.4 1.0 CD2 A:HIS499 3.0 12.6 1.0 CD2 A:HIS143 3.0 20.3 1.0 CE1 A:HIS499 3.0 15.2 1.0 CD2 A:HIS448 3.0 13.6 1.0 CE1 A:HIS143 3.0 15.4 1.0 CU A:CU703 3.5 30.4 1.0 O A:HOH2353 3.6 31.1 1.0 CD2 A:HIS446 3.6 11.8 1.0 NE2 A:HIS101 3.9 13.9 1.0 ND1 A:HIS448 4.0 15.0 1.0 CD2 A:HIS101 4.0 13.7 1.0 ND1 A:HIS499 4.1 13.2 1.0 CG A:HIS499 4.1 10.9 1.0 CG A:HIS448 4.1 12.2 1.0 ND1 A:HIS143 4.1 19.7 1.0 CG A:HIS143 4.1 15.2 1.0 NE2 A:HIS446 4.1 11.6 1.0 CB A:MET497 4.5 13.4 1.0 CE1 A:HIS101 4.6 18.9 1.0 CU3 A:C2O702 4.7 14.8 1.0 CG A:HIS101 4.7 11.4 1.0 CG A:HIS446 4.8 12.8 1.0 OE1 A:GLU506 4.9 20.0 1.0 CD2 A:HIS501 5.0 13.9 1.0 CE1 A:HIS141 5.0 11.7 1.0

Copper binding site 4 out of 4 in the Crystal Structure of Cueo, A Multi-Copper Oxidase From E. Coli Involved in Copper Homeostasis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Cueo, A Multi-Copper Oxidase From E. Coli Involved in Copper Homeostasis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu702 b:14.8 occ:1.00 CU3 A:C2O702 0.0 14.8 1.0 ND1 A:HIS103 2.0 10.7 1.0 NE2 A:HIS141 2.0 12.9 1.0 NE2 A:HIS501 2.1 11.6 1.0 O1 A:C2O702 2.4 14.2 1.0 CE1 A:HIS103 2.8 7.7 1.0 CE1 A:HIS141 2.9 11.7 1.0 CD2 A:HIS141 3.0 9.8 1.0 CE1 A:HIS501 3.0 13.2 1.0 CD2 A:HIS501 3.1 13.9 1.0 CG A:HIS103 3.1 8.4 1.0 CB A:HIS103 3.5 9.1 1.0 CZ2 A:TRP139 3.7 8.3 1.0 O A:HOH2353 3.9 31.1 1.0 CU A:CU703 4.0 30.4 1.0 NE2 A:HIS103 4.0 10.4 1.0 CE2 A:TRP139 4.1 7.2 1.0 ND1 A:HIS141 4.1 13.3 1.0 CD2 A:HIS103 4.1 9.3 1.0 CG A:HIS141 4.1 9.2 1.0 CD2 A:HIS101 4.1 13.7 1.0 NE1 A:TRP139 4.2 10.1 1.0 ND1 A:HIS501 4.2 13.6 1.0 CG A:HIS501 4.2 11.2 1.0 CD2 A:HIS446 4.3 11.8 1.0 NE2 A:HIS446 4.4 11.6 1.0 CH2 A:TRP139 4.4 9.8 1.0 NE2 A:HIS101 4.5 13.9 1.0 CU2 A:C2O702 4.7 22.5 1.0 CA A:HIS103 4.8 10.6 1.0

S.A.Roberts, A.Weichsel, G.Grass, K.Thakali, J.T.Hazzard, G.Tollin, C.Rensing, W.R.Montfort. Crystal Structure and Electron Transfer Kinetics of Cueo, A Multicopper Oxidase Required For Copper Homeostasis in Escherichia Coli. Proc.Natl.Acad.Sci.Usa V. 99 2766 2002.
ISSN: ISSN 0027-8424
PubMed: 11867755
DOI: 10.1073/PNAS.052710499