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Zinc in PDB 3aso: Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 0.9 Angstrom Wavelength

Enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 0.9 Angstrom Wavelength

All present enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 0.9 Angstrom Wavelength:
1.9.3.1;

Protein crystallography data

The structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 0.9 Angstrom Wavelength, PDB code: 3aso was solved by M.Suga, N.Yano, K.Muramoto, K.Shinzawa-Itoh, T.Maeda, E.Yamashita, T.Tsukihara, S.Yoshikawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 181.874, 204.106, 177.874, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 20.5

Other elements in 3aso:

The structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 0.9 Angstrom Wavelength also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Sodium (Na) 2 atoms
Copper (Cu) 6 atoms
Iron (Fe) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 0.9 Angstrom Wavelength (pdb code 3aso). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 0.9 Angstrom Wavelength, PDB code: 3aso:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3aso

Go back to Zinc Binding Sites List in 3aso
Zinc binding site 1 out of 2 in the Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 0.9 Angstrom Wavelength


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 0.9 Angstrom Wavelength within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Zn99

b:23.1
occ:1.00
SG F:CYS62 2.3 22.9 1.0
SG F:CYS60 2.3 21.6 1.0
SG F:CYS85 2.4 21.5 1.0
SG F:CYS82 2.4 20.3 1.0
CB F:CYS82 3.1 22.6 1.0
CB F:CYS60 3.3 20.3 1.0
CB F:CYS85 3.4 23.3 1.0
CB F:CYS62 3.4 23.2 1.0
CA F:CYS62 3.6 25.5 1.0
N F:CYS85 3.8 22.9 1.0
N F:CYS62 4.1 25.7 1.0
CA F:CYS85 4.2 24.4 1.0
O F:CYS60 4.4 22.7 1.0
C F:CYS60 4.5 21.6 1.0
CA F:CYS60 4.5 19.6 1.0
O F:HOH2514 4.6 36.0 1.0
CA F:CYS82 4.6 22.5 1.0
OG F:SER84 4.6 25.4 1.0
CG2 F:THR87 4.8 28.4 1.0
CB F:SER84 4.8 21.8 1.0
C F:SER84 4.8 22.3 1.0
CG1 F:ILE70 4.9 18.2 1.0
C F:CYS85 4.9 25.4 1.0
C F:ILE61 4.9 24.5 1.0
C F:CYS62 5.0 27.4 1.0
CB F:ILE70 5.0 19.0 1.0
N F:SER84 5.0 22.1 1.0

Zinc binding site 2 out of 2 in 3aso

Go back to Zinc Binding Sites List in 3aso
Zinc binding site 2 out of 2 in the Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 0.9 Angstrom Wavelength


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 0.9 Angstrom Wavelength within 5.0Å range:
probe atom residue distance (Å) B Occ
S:Zn99

b:23.7
occ:1.00
SG S:CYS85 2.3 20.3 1.0
SG S:CYS82 2.3 22.9 1.0
SG S:CYS60 2.4 19.1 1.0
SG S:CYS62 2.4 25.1 1.0
CB S:CYS82 3.1 21.1 1.0
CB S:CYS62 3.2 24.2 1.0
CB S:CYS60 3.3 16.6 1.0
CB S:CYS85 3.4 20.7 1.0
CA S:CYS62 3.7 25.2 1.0
N S:CYS85 3.7 21.8 1.0
CA S:CYS85 4.1 21.9 1.0
N S:CYS62 4.2 23.7 1.0
O S:CYS60 4.4 21.1 1.0
C S:CYS60 4.4 20.5 1.0
CA S:CYS60 4.5 19.2 1.0
OG1 S:THR87 4.5 29.3 1.0
O S:HOH3514 4.6 33.2 1.0
CA S:CYS82 4.6 21.0 1.0
CB S:SER84 4.6 23.6 1.0
OG S:SER84 4.6 27.2 1.0
C S:SER84 4.7 21.9 1.0
CG2 S:THR87 4.8 28.9 1.0
C S:CYS85 4.9 22.1 1.0
C S:ILE61 5.0 23.4 1.0
CA S:SER84 5.0 22.8 1.0
N S:SER84 5.0 22.8 1.0
N S:GLY86 5.0 22.8 1.0
CB S:ILE70 5.0 19.5 1.0
CG1 S:ILE70 5.0 17.8 1.0

Reference:

M.Suga, N.Yano, K.Muramoto, K.Shinzawa-Itoh, T.Maeda, E.Yamashita, T.Tsukihara, S.Yoshikawa. Distinguishing Between Cl- and O2(2-) As the Bridging Element Between FE3+ and CU2+ in Resting-Oxidized Cytochrome C Oxidase Acta Crystallogr.,Sect.D V. 67 742 2011.
ISSN: ISSN 0907-4449
PubMed: 21795816
DOI: 10.1107/S0907444911022803
Page generated: Wed Dec 16 04:07:38 2020

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