Copper in PDB 4e9q: Multicopper Oxidase Cueo (DATA2)

The structure of Multicopper Oxidase Cueo (DATA2), PDB code: 4e9q was solved by H.Komori, K.Kataoka, T.Sakurai, Y.Higuchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.386, 90.748, 53.304, 90.00, 102.68, 90.00
R / Rfree (%)	13.7 / n/a

The binding sites of Copper atom in the Multicopper Oxidase Cueo (DATA2) (pdb code 4e9q). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 5 binding sites of Copper where determined in the Multicopper Oxidase Cueo (DATA2), PDB code: 4e9q:
Jump to Copper binding site number: 1; 2; 3; 4; 5;

Copper binding site 1 out of 5 in the Multicopper Oxidase Cueo (DATA2)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Multicopper Oxidase Cueo (DATA2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1001 b:10.1 occ:1.00 ND1 A:HIS443 2.0 9.5 1.0 ND1 A:HIS505 2.0 8.5 1.0 SG A:CYS500 2.2 9.4 1.0 CE1 A:HIS505 3.0 9.5 1.0 CG A:HIS443 3.0 10.1 1.0 CE1 A:HIS443 3.0 9.8 1.0 CG A:HIS505 3.1 9.1 1.0 SD A:MET510 3.2 10.9 1.0 CB A:CYS500 3.2 9.4 1.0 CB A:HIS505 3.3 9.0 1.0 CB A:HIS443 3.4 10.0 1.0 O A:LEU442 3.6 10.8 1.0 CA A:HIS443 3.6 8.7 1.0 CE A:MET510 4.0 11.9 1.0 CB A:LEU502 4.1 7.4 1.0 NE2 A:HIS443 4.1 10.5 1.0 NE2 A:HIS505 4.1 9.5 1.0 CD2 A:HIS443 4.1 10.4 1.0 CD2 A:HIS505 4.2 9.5 1.0 C A:LEU442 4.4 9.9 1.0 N A:HIS443 4.4 8.7 1.0 CA A:CYS500 4.6 8.4 1.0 CG A:MET510 4.7 10.7 1.0 CD1 A:LEU502 4.8 9.4 1.0 C A:HIS443 4.8 8.3 1.0 CA A:HIS505 4.9 8.8 1.0 CG A:LEU502 4.9 7.1 1.0 O A:LEU502 4.9 8.2 1.0

Copper binding site 2 out of 5 in the Multicopper Oxidase Cueo (DATA2)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Multicopper Oxidase Cueo (DATA2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1002 b:7.2 occ:0.68 CU A:CU1002 0.0 7.2 0.7 CU A:CU1002 1.1 11.8 0.2 O A:HOH1101 2.0 9.8 0.9 ND1 A:HIS103 2.0 8.1 1.0 NE2 A:HIS501 2.1 8.7 1.0 O A:HOH1102 2.2 13.9 0.9 NE2 A:HIS141 2.2 10.3 1.0 CE1 A:HIS103 2.9 8.9 1.0 CD2 A:HIS501 3.0 8.7 1.0 CE1 A:HIS141 3.0 11.0 1.0 CE1 A:HIS501 3.2 9.3 1.0 CG A:HIS103 3.2 7.3 1.0 CD2 A:HIS141 3.4 9.7 1.0 CU A:CU1003 3.4 10.7 0.9 CB A:HIS103 3.6 8.1 1.0 CD2 A:HIS446 3.8 8.9 1.0 CU A:CU1004 3.8 9.1 0.8 NE2 A:HIS446 3.9 11.2 1.0 O A:HOH1103 4.0 15.2 1.0 CD2 A:HIS101 4.0 10.7 1.0 NE2 A:HIS103 4.1 8.1 1.0 CD2 A:HIS103 4.2 7.7 1.0 CG A:HIS501 4.2 7.5 1.0 ND1 A:HIS501 4.2 8.3 1.0 ND1 A:HIS141 4.2 9.9 1.0 NE2 A:HIS101 4.4 11.2 1.0 CZ2 A:TRP139 4.4 7.4 1.0 CG A:HIS141 4.4 9.8 1.0 CE1 A:HIS499 4.4 9.4 1.0 NE2 A:HIS499 4.5 9.4 1.0 CG A:HIS446 4.7 8.8 1.0 NE2 A:HIS143 4.7 10.6 1.0 CA A:HIS103 4.8 8.2 1.0 CE2 A:TRP139 4.8 7.5 1.0 NE1 A:TRP139 4.8 7.6 1.0 CE1 A:HIS446 4.9 11.5 1.0 NE2 A:HIS448 4.9 9.2 1.0

Copper binding site 3 out of 5 in the Multicopper Oxidase Cueo (DATA2)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Multicopper Oxidase Cueo (DATA2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1002 b:11.8 occ:0.22 CU A:CU1002 0.0 11.8 0.2 CU A:CU1002 1.1 7.2 0.7 NE2 A:HIS141 1.8 10.3 1.0 ND1 A:HIS103 1.9 8.1 1.0 NE2 A:HIS501 2.1 8.7 1.0 CD2 A:HIS141 2.7 9.7 1.0 CE1 A:HIS501 2.9 9.3 1.0 O A:HOH1101 2.9 9.8 0.9 CE1 A:HIS103 2.9 8.9 1.0 CE1 A:HIS141 2.9 11.0 1.0 CG A:HIS103 2.9 7.3 1.0 O A:HOH1102 3.1 13.9 0.9 CD2 A:HIS501 3.3 8.7 1.0 CB A:HIS103 3.3 8.1 1.0 CZ2 A:TRP139 3.4 7.4 1.0 CE2 A:TRP139 3.8 7.5 1.0 CG A:HIS141 3.8 9.8 1.0 ND1 A:HIS141 3.9 9.9 1.0 NE1 A:TRP139 4.0 7.6 1.0 NE2 A:HIS103 4.0 8.1 1.0 CD2 A:HIS103 4.0 7.7 1.0 ND1 A:HIS501 4.1 8.3 1.0 CH2 A:TRP139 4.1 8.7 1.0 CG A:HIS501 4.3 7.5 1.0 O A:HOH1103 4.4 15.2 1.0 CU A:CU1003 4.4 10.7 0.9 CD2 A:HIS101 4.5 10.7 1.0 CU A:CU1004 4.5 9.1 0.8 CD2 A:HIS446 4.6 8.9 1.0 CA A:HIS103 4.7 8.2 1.0 NE2 A:HIS446 4.7 11.2 1.0 CD2 A:TRP139 4.8 7.6 1.0 NE2 A:HIS101 4.9 11.2 1.0

Copper binding site 4 out of 5 in the Multicopper Oxidase Cueo (DATA2)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Multicopper Oxidase Cueo (DATA2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1003 b:10.7 occ:0.90 O A:HOH1101 1.9 9.8 0.9 NE2 A:HIS448 2.0 9.2 1.0 NE2 A:HIS143 2.1 10.6 1.0 NE2 A:HIS499 2.1 9.4 1.0 O A:HOH1102 2.3 13.9 0.9 CE1 A:HIS448 2.9 10.8 1.0 CE1 A:HIS499 3.0 9.4 1.0 CE1 A:HIS143 3.0 9.9 1.0 CD2 A:HIS448 3.1 10.3 1.0 CD2 A:HIS143 3.1 9.4 1.0 CD2 A:HIS499 3.2 10.2 1.0 CU A:CU1002 3.4 7.2 0.7 CD2 A:HIS446 3.5 8.9 1.0 CU A:CU1004 3.7 9.1 0.8 O A:HOH1103 3.8 15.2 1.0 CD2 A:HIS101 3.9 10.7 1.0 NE2 A:HIS101 4.0 11.2 1.0 NE2 A:HIS446 4.0 11.2 1.0 ND1 A:HIS448 4.1 10.3 1.0 ND1 A:HIS499 4.1 9.3 1.0 ND1 A:HIS143 4.2 10.4 1.0 CG A:HIS448 4.2 10.3 1.0 CG A:HIS143 4.3 9.8 1.0 CG A:HIS499 4.3 9.5 1.0 CE1 A:HIS141 4.3 11.0 1.0 CU A:CU1002 4.4 11.8 0.2 NE2 A:HIS141 4.5 10.3 1.0 NE2 A:HIS501 4.5 8.7 1.0 CD2 A:HIS501 4.6 8.7 1.0 CG A:HIS101 4.7 10.4 1.0 CE1 A:HIS101 4.8 10.3 1.0 CG A:HIS446 4.8 8.8 1.0 OE2 A:GLU506 4.8 27.0 1.0 CB A:MET497 4.9 10.5 1.0 ND1 A:HIS103 4.9 8.1 1.0

Copper binding site 5 out of 5 in the Multicopper Oxidase Cueo (DATA2)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Multicopper Oxidase Cueo (DATA2) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1004 b:9.1 occ:0.75 O A:HOH1102 1.9 13.9 0.9 NE2 A:HIS446 2.0 11.2 1.0 NE2 A:HIS101 2.0 11.2 1.0 OXT A:ACT1005 2.1 16.3 0.5 O A:HOH1104 2.1 12.9 0.5 CE1 A:HIS101 2.9 10.3 1.0 CE1 A:HIS446 2.9 11.5 1.0 CD2 A:HIS446 3.0 8.9 1.0 C A:ACT1005 3.0 13.3 0.5 CD2 A:HIS101 3.0 10.7 1.0 CD2 A:HIS448 3.2 10.3 1.0 O A:ACT1005 3.3 12.2 0.5 NE2 A:HIS448 3.3 9.2 1.0 CA A:HIS103 3.5 8.2 1.0 CG A:HIS103 3.5 7.3 1.0 ND1 A:HIS103 3.7 8.1 1.0 CU A:CU1003 3.7 10.7 0.9 CB A:HIS103 3.7 8.1 1.0 CG A:HIS448 3.7 10.3 1.0 CU A:CU1002 3.8 7.2 0.7 CE1 A:HIS448 3.9 10.8 1.0 ND1 A:HIS101 4.1 11.1 1.0 CD2 A:HIS103 4.1 7.7 1.0 ND1 A:HIS446 4.1 11.3 1.0 CG A:HIS446 4.1 8.8 1.0 ND1 A:HIS448 4.1 10.3 1.0 CG A:HIS101 4.1 10.4 1.0 N A:GLY104 4.1 8.8 1.0 O A:HOH1101 4.2 9.8 0.9 CE1 A:HIS103 4.2 8.9 1.0 CH3 A:ACT1005 4.3 22.4 0.5 C A:HIS103 4.4 8.2 1.0 NE2 A:HIS103 4.4 8.1 1.0 N A:HIS103 4.5 7.6 1.0 CU A:CU1002 4.5 11.8 0.2 CA A:HIS448 4.5 11.1 1.0 O A:HOH1105 4.5 12.0 0.5 O A:HOH1106 4.6 9.4 0.5 CB A:HIS448 4.6 10.4 1.0 O A:TRP102 4.6 10.5 1.0 C A:TRP102 4.9 7.3 1.0 N A:HIS448 5.0 11.9 1.0

K.Kataoka, H.Komori, Y.Ueki, Y.Konno, Y.Kamitaka, S.Kurose, S.Tsujimura, Y.Higuchi, K.Kano, D.Seo, T.Sakurai. Structure and Function of the Engineered Multicopper Oxidase Cueo From Escherichia Coli--Deletion of the Methionine-Rich Helical Region Covering the Substrate-Binding Site. J.Mol.Biol. V. 373 141 2007.
ISSN: ISSN 0022-2836
PubMed: 17804014
DOI: 10.1016/J.JMB.2007.07.041