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Zinc in PDB 3asn: Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 Angstrom Wavelength

Enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 Angstrom Wavelength

All present enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 Angstrom Wavelength:
1.9.3.1;

Protein crystallography data

The structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 Angstrom Wavelength, PDB code: 3asn 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 / 3.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 181.826, 204.098, 177.829, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 18.7

Other elements in 3asn:

The structure of Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 Angstrom Wavelength also contains other interesting chemical elements:

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

Zinc Binding Sites:

The binding sites of Zinc atom in the Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 Angstrom Wavelength (pdb code 3asn). 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 1.7470 Angstrom Wavelength, PDB code: 3asn:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3asn

Go back to Zinc Binding Sites List in 3asn
Zinc binding site 1 out of 2 in the Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 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 1.7470 Angstrom Wavelength within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Zn99

b:22.0
occ:1.00
SG F:CYS60 2.3 23.6 1.0
SG F:CYS62 2.3 19.9 1.0
SG F:CYS82 2.4 21.9 1.0
SG F:CYS85 2.4 22.4 1.0
CB F:CYS82 3.2 20.4 1.0
CB F:CYS60 3.3 17.6 1.0
CB F:CYS85 3.4 20.3 1.0
CB F:CYS62 3.4 21.7 1.0
CA F:CYS62 3.6 22.1 1.0
N F:CYS85 3.8 20.9 1.0
N F:CYS62 4.1 21.9 1.0
CA F:CYS85 4.2 21.2 1.0
O F:CYS60 4.2 19.6 1.0
C F:CYS60 4.4 18.6 1.0
CA F:CYS60 4.5 17.9 1.0
O F:HOH2514 4.5 28.1 1.0
CA F:CYS82 4.7 19.9 1.0
OG F:SER84 4.7 22.1 1.0
CB F:SER84 4.8 20.6 1.0
C F:SER84 4.8 20.6 1.0
C F:ILE61 4.9 20.8 1.0
CG2 F:THR87 4.9 26.3 1.0
CG1 F:ILE70 4.9 15.8 1.0
C F:CYS85 4.9 22.0 1.0
C F:CYS62 4.9 23.0 1.0
CB F:ILE70 5.0 16.2 1.0

Zinc binding site 2 out of 2 in 3asn

Go back to Zinc Binding Sites List in 3asn
Zinc binding site 2 out of 2 in the Bovine Heart Cytochrome C Oxidase in the Fully Oxidized State Measured at 1.7470 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 1.7470 Angstrom Wavelength within 5.0Å range:
probe atom residue distance (Å) B Occ
S:Zn99

b:22.7
occ:1.00
SG S:CYS62 2.3 25.3 1.0
SG S:CYS60 2.3 15.7 1.0
SG S:CYS85 2.4 19.6 1.0
SG S:CYS82 2.4 22.0 1.0
CB S:CYS82 3.2 18.0 1.0
CB S:CYS62 3.2 23.3 1.0
CB S:CYS60 3.3 16.4 1.0
CB S:CYS85 3.3 18.5 1.0
CA S:CYS62 3.6 23.9 1.0
N S:CYS85 3.7 18.3 1.0
N S:CYS62 4.1 22.5 1.0
CA S:CYS85 4.1 18.8 1.0
O S:CYS60 4.4 17.8 1.0
C S:CYS60 4.4 17.9 1.0
CA S:CYS60 4.4 16.8 1.0
OG1 S:THR87 4.6 24.9 1.0
OG S:SER84 4.6 20.2 1.0
CA S:CYS82 4.6 18.2 1.0
CB S:SER84 4.7 18.6 1.0
C S:SER84 4.7 18.4 1.0
O S:HOH3514 4.8 37.1 1.0
C S:ILE61 4.9 21.2 1.0
C S:CYS85 4.9 19.6 1.0
CB S:ILE70 5.0 16.2 1.0
C S:CYS62 5.0 25.6 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 04:07:35 2020

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