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Copper in PDB 5zco: Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days

Enzymatic activity of Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days

All present enzymatic activity of Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days:
1.9.3.1;

Protein crystallography data

The structure of Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days, PDB code: 5zco was solved by A.Shimada, K.Hatano, H.Tadehara, T.Tsukihara, 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 (°) 183.379, 206.655, 177.589, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 18.9

Other elements in 5zco:

The structure of Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Zinc (Zn) 2 atoms
Iron (Fe) 6 atoms
Sodium (Na) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days (pdb code 5zco). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days, PDB code: 5zco:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 5zco

Go back to Copper Binding Sites List in 5zco
Copper binding site 1 out of 6 in the Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu603

b:28.1
occ:1.00
N1 A:AZI607 1.9 21.9 0.3
NE2 A:HIS291 2.0 25.4 1.0
ND1 A:HIS240 2.0 26.6 1.0
NE2 A:HIS290 2.0 26.9 1.0
N3 A:AZI607 2.2 29.2 0.7
N2 A:AZI607 2.4 27.9 0.7
N2 A:AZI607 2.6 30.1 0.3
CE1 A:HIS291 2.9 22.7 1.0
CD2 A:HIS291 3.0 26.4 1.0
CG A:HIS240 3.0 24.8 1.0
CE1 A:HIS290 3.0 25.7 1.0
CD2 A:HIS290 3.0 25.5 1.0
CE1 A:HIS240 3.1 25.0 1.0
N3 A:AZI606 3.1 21.5 0.3
N1 A:AZI607 3.2 25.9 0.7
CB A:HIS240 3.3 22.7 1.0
N2 A:AZI606 3.5 25.0 0.3
N3 A:AZI607 3.7 26.1 0.3
CA A:HIS240 3.9 23.2 1.0
ND1 A:HIS291 4.0 24.4 1.0
CG A:HIS291 4.1 26.2 1.0
ND1 A:HIS290 4.1 25.6 1.0
CD2 A:HIS240 4.2 24.5 1.0
NE2 A:HIS240 4.2 24.3 1.0
CG A:HIS290 4.2 27.3 1.0
N1 A:AZI606 4.2 26.3 0.3
C1A A:HEA602 4.6 22.1 0.7
NA A:HEA602 4.7 24.4 0.7
N A:HIS240 4.7 22.8 1.0
ND A:HEA602 4.8 24.7 0.3
C4A A:HEA602 4.8 22.9 0.7
C2A A:HEA602 4.9 21.5 0.7
C4D A:HEA602 4.9 24.7 0.3
CG2 A:VAL243 4.9 24.3 1.0
C1A A:HEA602 4.9 25.3 0.3
CHA A:HEA602 5.0 23.3 0.7
NA A:HEA602 5.0 25.6 0.3
CHA A:HEA602 5.0 24.6 0.3
C A:HIS240 5.0 22.9 1.0
C3A A:HEA602 5.0 23.6 0.7

Copper binding site 2 out of 6 in 5zco

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Copper binding site 2 out of 6 in the Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu303

b:29.8
occ:1.00
CU1 B:CUA303 0.0 29.8 1.0
ND1 B:HIS161 2.0 26.4 1.0
SG B:CYS196 2.3 27.4 1.0
SG B:CYS200 2.3 28.4 1.0
SD B:MET207 2.4 29.7 1.0
CU2 B:CUA303 2.5 28.4 1.0
O B:HOH401 2.9 76.0 1.0
CE1 B:HIS161 3.0 25.4 1.0
CE B:MET207 3.1 27.5 1.0
CG B:HIS161 3.2 28.9 1.0
CB B:CYS200 3.3 28.8 1.0
CB B:CYS196 3.4 28.2 1.0
O B:HOH403 3.5 98.5 1.0
CG B:MET207 3.6 30.2 1.0
CB B:HIS161 3.6 24.6 1.0
O B:GLU198 4.0 28.1 1.0
NE2 B:HIS161 4.2 26.9 1.0
CA B:HIS161 4.2 25.4 1.0
CD2 B:HIS161 4.3 26.0 1.0
ND1 B:HIS204 4.4 30.3 1.0
CA B:HIS204 4.7 28.3 1.0
CD1 B:TRP104 4.7 27.6 1.0
O B:LEU160 4.7 25.5 1.0
O B:HIS102 4.7 29.1 1.0
CA B:CYS200 4.8 28.5 1.0
CA B:CYS196 4.8 28.7 1.0
CB B:MET207 4.9 29.3 1.0
O B:HIS204 4.9 30.6 1.0

Copper binding site 3 out of 6 in 5zco

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Copper binding site 3 out of 6 in the Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu303

b:28.4
occ:1.00
CU2 B:CUA303 0.0 28.4 1.0
ND1 B:HIS204 2.0 30.3 1.0
SG B:CYS196 2.3 27.4 1.0
SG B:CYS200 2.3 28.4 1.0
O B:GLU198 2.3 28.1 1.0
CU1 B:CUA303 2.5 29.8 1.0
CE1 B:HIS204 2.9 30.9 1.0
CG B:HIS204 3.1 27.6 1.0
O B:HOH401 3.2 76.0 1.0
CB B:CYS200 3.4 28.8 1.0
CB B:CYS196 3.4 28.2 1.0
C B:GLU198 3.4 25.9 1.0
CB B:HIS204 3.5 27.4 1.0
CA B:HIS204 3.6 28.3 1.0
N B:CYS200 3.7 27.4 1.0
O B:HIS204 3.8 30.6 1.0
O B:HOH403 3.9 98.5 1.0
NE2 B:HIS204 4.0 27.8 1.0
N B:GLU198 4.1 25.6 1.0
C B:ILE199 4.1 26.6 1.0
CD2 B:HIS204 4.1 26.7 1.0
ND1 B:HIS161 4.1 26.4 1.0
C B:HIS204 4.2 27.9 1.0
CA B:CYS200 4.2 28.5 1.0
C B:CYS196 4.2 28.0 1.0
N B:ILE199 4.2 28.8 1.0
O B:CYS196 4.3 26.6 1.0
CA B:ILE199 4.3 28.6 1.0
SD B:MET207 4.3 29.7 1.0
CA B:CYS196 4.5 28.7 1.0
CA B:GLU198 4.5 27.5 1.0
N B:SER197 4.6 27.3 1.0
CG B:MET207 4.7 30.2 1.0
N B:HIS204 4.9 30.6 1.0
CA B:HIS161 4.9 25.4 1.0
O B:ILE199 5.0 26.3 1.0

Copper binding site 4 out of 6 in 5zco

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Copper binding site 4 out of 6 in the Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Cu604

b:31.0
occ:1.00
NE2 N:HIS291 1.9 31.1 1.0
ND1 N:HIS240 2.0 29.5 1.0
NE2 N:HIS290 2.0 28.7 1.0
N1 N:AZI608 2.2 22.9 0.3
N3 N:AZI608 2.2 33.6 0.7
N2 N:AZI608 2.6 25.8 0.7
CE1 N:HIS291 2.9 27.7 1.0
CE1 N:HIS290 3.0 27.7 1.0
CG N:HIS240 3.0 28.2 1.0
CE1 N:HIS240 3.0 27.3 1.0
CD2 N:HIS291 3.0 31.2 1.0
N2 N:AZI608 3.0 22.4 0.3
CD2 N:HIS290 3.1 27.3 1.0
N3 N:AZI607 3.1 23.2 0.3
CB N:HIS240 3.3 26.8 1.0
N1 N:AZI608 3.4 30.7 0.7
N2 N:AZI607 3.5 23.1 0.3
CA N:HIS240 3.8 28.0 1.0
ND1 N:HIS291 4.0 29.4 1.0
CG N:HIS291 4.1 29.2 1.0
N3 N:AZI608 4.1 23.0 0.3
NE2 N:HIS240 4.1 26.4 1.0
ND1 N:HIS290 4.1 26.9 1.0
CD2 N:HIS240 4.1 26.4 1.0
N1 N:AZI607 4.2 22.4 0.3
CG N:HIS290 4.2 29.2 1.0
C1A N:HEA603 4.6 24.4 0.7
NA N:HEA603 4.6 26.1 0.7
N N:HIS240 4.7 25.7 1.0
ND N:HEA603 4.8 29.1 0.3
C4A N:HEA603 4.8 25.2 0.7
C4D N:HEA603 4.8 28.9 0.3
C2A N:HEA603 4.9 26.5 0.7
CG2 N:VAL243 4.9 29.2 1.0
C1A N:HEA603 4.9 30.0 0.3
CHA N:HEA603 4.9 25.0 0.7
CHA N:HEA603 4.9 28.6 0.3
C3A N:HEA603 4.9 24.3 0.7
C N:HIS240 5.0 28.0 1.0
NA N:HEA603 5.0 30.3 0.3
FE N:HEA603 5.0 30.9 0.3
FE N:HEA603 5.0 26.8 0.7

Copper binding site 5 out of 6 in 5zco

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Copper binding site 5 out of 6 in the Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Cu301

b:34.3
occ:1.00
CU1 O:CUA301 0.0 34.3 1.0
ND1 O:HIS161 2.1 33.4 1.0
SG O:CYS196 2.3 33.7 1.0
SG O:CYS200 2.3 32.6 1.0
SD O:MET207 2.4 35.3 1.0
CU2 O:CUA301 2.5 33.5 1.0
CE1 O:HIS161 3.0 31.3 1.0
CG O:HIS161 3.1 31.3 1.0
CB O:CYS200 3.2 29.4 1.0
CE O:MET207 3.2 34.0 1.0
CB O:CYS196 3.4 34.1 1.0
CB O:HIS161 3.6 28.9 1.0
CG O:MET207 3.6 33.9 1.0
O O:GLU198 3.9 30.4 1.0
NE2 O:HIS161 4.2 33.9 1.0
CA O:HIS161 4.2 32.0 1.0
CD2 O:HIS161 4.2 32.1 1.0
ND1 O:HIS204 4.4 34.8 1.0
CA O:CYS200 4.6 32.8 1.0
CD1 O:TRP104 4.7 36.9 1.0
O O:HIS102 4.7 35.0 1.0
O O:LEU160 4.7 32.1 1.0
CA O:HIS204 4.7 36.1 1.0
CA O:CYS196 4.8 34.4 1.0
CB O:MET207 4.9 34.0 1.0
O O:HIS204 5.0 36.4 1.0

Copper binding site 6 out of 6 in 5zco

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Copper binding site 6 out of 6 in the Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Azide-Bound Cytochrome C Oxidase Structure Determined Using the Crystals Exposed to 2 Mm Azide Solution For 2 Days within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Cu301

b:33.5
occ:1.00
CU2 O:CUA301 0.0 33.5 1.0
ND1 O:HIS204 2.0 34.8 1.0
O O:GLU198 2.3 30.4 1.0
SG O:CYS200 2.3 32.6 1.0
SG O:CYS196 2.3 33.7 1.0
CU1 O:CUA301 2.5 34.3 1.0
CE1 O:HIS204 2.8 36.7 1.0
CG O:HIS204 3.1 31.9 1.0
CB O:CYS200 3.3 29.4 1.0
CB O:CYS196 3.3 34.1 1.0
C O:GLU198 3.4 28.0 1.0
CB O:HIS204 3.6 34.0 1.0
CA O:HIS204 3.6 36.1 1.0
N O:CYS200 3.7 35.3 1.0
O O:HIS204 3.9 36.4 1.0
NE2 O:HIS204 4.0 33.9 1.0
N O:GLU198 4.1 30.6 1.0
CA O:CYS200 4.1 32.8 1.0
C O:ILE199 4.1 36.2 1.0
ND1 O:HIS161 4.2 33.4 1.0
CD2 O:HIS204 4.2 31.0 1.0
N O:ILE199 4.2 32.9 1.0
C O:CYS196 4.2 35.3 1.0
C O:HIS204 4.2 33.4 1.0
O O:CYS196 4.2 33.3 1.0
CA O:ILE199 4.2 34.0 1.0
SD O:MET207 4.3 35.3 1.0
CA O:CYS196 4.4 34.4 1.0
CA O:GLU198 4.4 34.5 1.0
N O:SER197 4.6 34.8 1.0
CG O:MET207 4.7 33.9 1.0
N O:HIS204 4.9 34.0 1.0
CA O:HIS161 4.9 32.0 1.0
CG O:HIS161 5.0 31.3 1.0
O O:ILE199 5.0 32.5 1.0
CB O:HIS161 5.0 28.9 1.0

Reference:

A.Shimada, K.Hatano, H.Tadehara, N.Yano, K.Shinzawa-Itoh, E.Yamashita, K.Muramoto, T.Tsukihara, S.Yoshikawa. X-Ray Structural Analyses of Azide-Bound Cytochromecoxidases Reveal That the H-Pathway Is Critically Important For the Proton-Pumping Activity. J. Biol. Chem. V. 293 14868 2018.
ISSN: ESSN 1083-351X
PubMed: 30077971
DOI: 10.1074/JBC.RA118.003123
Page generated: Wed Jul 31 05:36:35 2024

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