Atomistry » Copper » PDB 2cj3-2foy » 2eij
Atomistry »
  Copper »
    PDB 2cj3-2foy »
      2eij »

Copper in PDB 2eij: Bovine Heart Cytochrome C Oxidase in the Fully Reduced State

Enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Fully Reduced State

All present enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Fully Reduced State:
1.9.3.1;

Protein crystallography data

The structure of Bovine Heart Cytochrome C Oxidase in the Fully Reduced State, PDB code: 2eij was solved by K.Muramoto, K.Hirata, K.Shinzawa-Itoh, S.Yoko-O, E.Yamashita, H.Aoyama, T.Tsukihara, S.Yoshikawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 183.060, 206.584, 178.298, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 23.4

Other elements in 2eij:

The structure of Bovine Heart Cytochrome C Oxidase in the Fully Reduced State also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Zinc (Zn) 4 atoms
Iron (Fe) 4 atoms
Sodium (Na) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Bovine Heart Cytochrome C Oxidase in the Fully Reduced State (pdb code 2eij). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Bovine Heart Cytochrome C Oxidase in the Fully Reduced State, PDB code: 2eij:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 2eij

Go back to Copper Binding Sites List in 2eij
Copper binding site 1 out of 6 in the Bovine Heart Cytochrome C Oxidase in the Fully Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Bovine Heart Cytochrome C Oxidase in the Fully Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu517

b:18.0
occ:1.00
 NE2 A:HIS291 1.9 19.7 1.0
ND1 A:HIS240 2.0 20.0 1.0
NE2 A:HIS290 2.0 17.8 1.0
CD2 A:HIS291 2.9 17.1 1.0
CG A:HIS240 3.0 15.9 1.0
CE1 A:HIS290 3.0 15.5 1.0
CE1 A:HIS291 3.0 17.1 1.0
CE1 A:HIS240 3.0 18.2 1.0
CD2 A:HIS290 3.1 15.9 1.0
CB A:HIS240 3.3 12.6 1.0
CA A:HIS240 3.9 13.9 1.0
CG A:HIS291 4.1 19.3 1.0
ND1 A:HIS291 4.1 17.3 1.0
CD2 A:HIS240 4.1 18.0 1.0
NE2 A:HIS240 4.1 20.7 1.0
ND1 A:HIS290 4.1 14.3 1.0
CG A:HIS290 4.2 16.4 1.0
NA A:HEA516 4.6 15.1 1.0
C1A A:HEA516 4.6 15.3 1.0
CG2 A:VAL243 4.7 11.6 1.0
N A:HIS240 4.7 12.9 1.0
C4A A:HEA516 4.8 16.2 1.0
C2A A:HEA516 4.8 15.7 1.0
CHA A:HEA516 4.9 14.8 1.0
C3A A:HEA516 5.0 15.8 1.0

Copper binding site 2 out of 6 in 2eij

Go back to Copper Binding Sites List in 2eij
Copper binding site 2 out of 6 in the Bovine Heart Cytochrome C Oxidase in the Fully Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Bovine Heart Cytochrome C Oxidase in the Fully Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu228

b:18.9
occ:1.00
 CU1 B:CUA228 0.0 18.9 1.0
ND1 B:HIS161 2.0 16.8 1.0
SG B:CYS196 2.2 17.4 1.0
SG B:CYS200 2.3 17.6 1.0
CU2 B:CUA228 2.5 17.7 1.0
SD B:MET207 2.6 18.4 1.0
CE1 B:HIS161 2.9 13.7 1.0
CE B:MET207 3.0 12.2 1.0
CG B:HIS161 3.2 12.6 1.0
CB B:CYS200 3.3 18.6 1.0
CB B:CYS196 3.4 13.8 1.0
CG B:MET207 3.6 18.3 1.0
CB B:HIS161 3.7 13.9 1.0
NE2 B:HIS161 4.1 13.8 1.0
CA B:HIS161 4.2 15.1 1.0
O B:GLU198 4.2 21.8 1.0
CD2 B:HIS161 4.3 14.1 1.0
ND1 B:HIS204 4.4 19.4 1.0
CD1 B:TRP104 4.5 16.9 1.0
O B:HIS102 4.7 17.7 1.0
O B:LEU160 4.7 17.2 1.0
CA B:CYS200 4.7 18.3 1.0
CA B:CYS196 4.8 16.2 1.0
CA B:HIS204 4.8 16.7 1.0
N B:CYS200 4.9 20.1 1.0
CB B:MET207 4.9 15.6 1.0
O B:HIS204 5.0 16.6 1.0

Copper binding site 3 out of 6 in 2eij

Go back to Copper Binding Sites List in 2eij
Copper binding site 3 out of 6 in the Bovine Heart Cytochrome C Oxidase in the Fully Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Bovine Heart Cytochrome C Oxidase in the Fully Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu228

b:17.7
occ:1.00
 CU2 B:CUA228 0.0 17.7 1.0
ND1 B:HIS204 2.0 19.4 1.0
SG B:CYS200 2.2 17.6 1.0
SG B:CYS196 2.3 17.4 1.0
CU1 B:CUA228 2.5 18.9 1.0
O B:GLU198 2.5 21.8 1.0
CE1 B:HIS204 2.9 16.3 1.0
CG B:HIS204 3.1 15.7 1.0
CB B:CYS196 3.3 13.8 1.0
CB B:CYS200 3.4 18.6 1.0
CB B:HIS204 3.5 14.8 1.0
CA B:HIS204 3.5 16.7 1.0
N B:CYS200 3.6 20.1 1.0
C B:GLU198 3.6 20.1 1.0
O B:HIS204 3.8 16.6 1.0
NE2 B:HIS204 4.0 18.3 1.0
O B:CYS196 4.1 16.9 1.0
C B:HIS204 4.1 17.1 1.0
CD2 B:HIS204 4.1 14.8 1.0
ND1 B:HIS161 4.1 16.8 1.0
CA B:CYS200 4.2 18.3 1.0
N B:GLU198 4.2 16.3 1.0
C B:CYS196 4.2 18.9 1.0
C B:ILE199 4.2 19.7 1.0
CA B:ILE199 4.3 17.9 1.0
CA B:CYS196 4.4 16.2 1.0
N B:ILE199 4.4 18.3 1.0
SD B:MET207 4.5 18.4 1.0
CA B:GLU198 4.6 17.0 1.0
CG B:MET207 4.7 18.3 1.0
N B:SER197 4.8 18.7 1.0
N B:HIS204 4.8 22.4 1.0
CA B:HIS161 4.9 15.1 1.0
CE1 B:HIS161 5.0 13.7 1.0

Copper binding site 4 out of 6 in 2eij

Go back to Copper Binding Sites List in 2eij
Copper binding site 4 out of 6 in the Bovine Heart Cytochrome C Oxidase in the Fully Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Bovine Heart Cytochrome C Oxidase in the Fully Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Cu517

b:20.0
occ:1.00
 NE2 N:HIS291 2.0 23.3 1.0
ND1 N:HIS240 2.0 19.0 1.0
NE2 N:HIS290 2.0 16.3 1.0
CD2 N:HIS291 2.9 26.1 1.0
CE1 N:HIS290 3.0 19.3 1.0
CG N:HIS240 3.0 21.6 1.0
CE1 N:HIS240 3.0 22.7 1.0
CE1 N:HIS291 3.0 24.6 1.0
CD2 N:HIS290 3.1 18.7 1.0
CB N:HIS240 3.3 17.8 1.0
CA N:HIS240 3.9 19.3 1.0
CG N:HIS291 4.1 26.1 1.0
CD2 N:HIS240 4.1 21.8 1.0
ND1 N:HIS291 4.1 25.6 1.0
NE2 N:HIS240 4.1 24.7 1.0
ND1 N:HIS290 4.1 15.9 1.0
CG N:HIS290 4.2 20.0 1.0
NA N:HEA516 4.6 18.9 1.0
C1A N:HEA516 4.6 19.6 1.0
N N:HIS240 4.7 17.8 1.0
CG2 N:VAL243 4.7 17.1 1.0
C4A N:HEA516 4.8 18.5 1.0
C2A N:HEA516 4.9 18.9 1.0
CHA N:HEA516 4.9 18.4 1.0
C3A N:HEA516 5.0 18.2 1.0

Copper binding site 5 out of 6 in 2eij

Go back to Copper Binding Sites List in 2eij
Copper binding site 5 out of 6 in the Bovine Heart Cytochrome C Oxidase in the Fully Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Bovine Heart Cytochrome C Oxidase in the Fully Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Cu228

b:25.6
occ:1.00
 CU1 O:CUA228 0.0 25.6 1.0
ND1 O:HIS161 2.0 25.9 1.0
SG O:CYS196 2.3 21.5 1.0
SG O:CYS200 2.3 22.1 1.0
CU2 O:CUA228 2.3 25.9 1.0
SD O:MET207 2.7 27.9 1.0
CE1 O:HIS161 2.9 24.6 1.0
CG O:HIS161 3.2 21.4 1.0
CE O:MET207 3.3 18.4 1.0
CB O:CYS200 3.3 25.2 1.0
CB O:CYS196 3.3 24.1 1.0
CG O:MET207 3.6 26.3 1.0
CB O:HIS161 3.7 20.8 1.0
NE2 O:HIS161 4.1 22.6 1.0
O O:GLU198 4.1 25.4 1.0
CA O:HIS161 4.2 20.3 1.0
CD2 O:HIS161 4.2 20.8 1.0
ND1 O:HIS204 4.3 27.8 1.0
CD1 O:TRP104 4.6 22.1 1.0
CA O:CYS196 4.7 23.7 1.0
CA O:CYS200 4.7 24.8 1.0
O O:LEU160 4.7 21.7 1.0
CA O:HIS204 4.8 23.3 1.0
O O:HIS102 4.8 21.6 1.0
N O:CYS200 4.9 27.4 1.0
O O:HIS204 4.9 25.0 1.0
CB O:MET207 5.0 25.6 1.0

Copper binding site 6 out of 6 in 2eij

Go back to Copper Binding Sites List in 2eij
Copper binding site 6 out of 6 in the Bovine Heart Cytochrome C Oxidase in the Fully Reduced State


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Bovine Heart Cytochrome C Oxidase in the Fully Reduced State within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Cu228

b:25.9
occ:1.00
 CU2 O:CUA228 0.0 25.9 1.0
ND1 O:HIS204 2.1 27.8 1.0
SG O:CYS196 2.2 21.5 1.0
SG O:CYS200 2.3 22.1 1.0
CU1 O:CUA228 2.3 25.6 1.0
O O:GLU198 2.5 25.4 1.0
CE1 O:HIS204 2.9 24.6 1.0
CG O:HIS204 3.2 25.2 1.0
CB O:CYS196 3.2 24.1 1.0
CB O:CYS200 3.4 25.2 1.0
N O:CYS200 3.6 27.4 1.0
C O:GLU198 3.6 22.4 1.0
CA O:HIS204 3.6 23.3 1.0
CB O:HIS204 3.7 22.6 1.0
O O:HIS204 3.9 25.0 1.0
ND1 O:HIS161 4.0 25.9 1.0
NE2 O:HIS204 4.1 24.1 1.0
CA O:CYS200 4.1 24.8 1.0
O O:CYS196 4.1 25.5 1.0
N O:GLU198 4.2 21.7 1.0
C O:HIS204 4.2 23.1 1.0
CD2 O:HIS204 4.2 21.6 1.0
C O:ILE199 4.2 26.8 1.0
C O:CYS196 4.2 26.5 1.0
CA O:ILE199 4.3 22.8 1.0
N O:ILE199 4.4 20.8 1.0
CA O:CYS196 4.4 23.7 1.0
SD O:MET207 4.5 27.9 1.0
CA O:GLU198 4.6 22.2 1.0
CG O:MET207 4.7 26.3 1.0
CE1 O:HIS161 4.8 24.6 1.0
N O:SER197 4.8 27.0 1.0
CA O:HIS161 4.8 20.3 1.0
N O:HIS204 4.8 24.0 1.0
CG O:HIS161 4.9 21.4 1.0

Reference:

K.Muramoto, K.Hirata, K.Shinzawa-Itoh, S.Yoko-O, E.Yamashita, H.Aoyama, T.Tsukihara, S.Yoshikawa. A Histidine Residue Acting As A Controlling Site For Dioxygen Reduction and Proton Pumping By Cytochrome C Oxidase Proc.Natl.Acad.Sci.Usa V. 104 7881 2007.
ISSN: ISSN 0027-8424
PubMed: 17470809
DOI: 10.1073/PNAS.0610031104
Page generated: Tue Jul 30 23:26:41 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy