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Copper in PDB 7xma: Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso

Enzymatic activity of Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso

All present enzymatic activity of Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso:
7.1.1.9;

Protein crystallography data

The structure of Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso, PDB code: 7xma was solved by Y.Nishida, K.Shinzawa-Itoh, N.Mizuno, T.Kumasaka, S.Yoshikawa, T.Tsukihara, S.Takashima, Y.Shintani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.97 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 181.8, 203.577, 177.859, 90, 90, 90
R / Rfree (%) 18.6 / 21.3

Other elements in 7xma:

The structure of Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso also contains other interesting chemical elements:

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

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso (pdb code 7xma). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso, PDB code: 7xma:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 7xma

Go back to Copper Binding Sites List in 7xma
Copper binding site 1 out of 6 in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu603

b:18.2
occ:1.00
NE2 A:HIS290 2.0 25.1 1.0
NE2 A:HIS291 2.0 28.7 1.0
ND1 A:HIS240 2.3 33.9 1.0
O2 A:PER606 2.3 36.1 1.0
O1 A:PER606 2.4 42.5 1.0
CE1 A:HIS290 2.9 35.2 1.0
CE1 A:HIS291 2.9 27.2 1.0
CD2 A:HIS291 2.9 24.2 1.0
CD2 A:HIS290 3.1 25.2 1.0
CG A:HIS240 3.1 42.6 1.0
CB A:HIS240 3.3 22.7 1.0
CE1 A:HIS240 3.3 42.6 1.0
CA A:HIS240 3.9 29.7 1.0
ND1 A:HIS291 4.0 25.9 1.0
CG A:HIS291 4.0 26.6 1.0
ND1 A:HIS290 4.1 25.4 1.0
CG A:HIS290 4.2 24.8 1.0
CD2 A:HIS240 4.3 22.9 1.0
NE2 A:HIS240 4.4 43.6 1.0
NA A:HEA602 4.5 34.0 1.0
C1A A:HEA602 4.6 21.3 1.0
N A:HIS240 4.7 19.9 1.0
C4A A:HEA602 4.8 19.7 1.0
CG2 A:VAL243 4.9 22.1 1.0
FE A:HEA602 4.9 25.4 1.0
O A:VAL287 5.0 33.7 1.0
CHA A:HEA602 5.0 21.8 1.0
C2A A:HEA602 5.0 39.8 1.0

Copper binding site 2 out of 6 in 7xma

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Copper binding site 2 out of 6 in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu601

b:17.9
occ:1.00
CU1 B:CUA601 0.0 17.9 1.0
ND1 B:HIS161 2.0 23.7 1.0
SG B:CYS200 2.3 26.3 1.0
SG B:CYS196 2.3 23.6 1.0
SD B:MET207 2.4 30.6 1.0
CU2 B:CUA601 2.5 20.1 1.0
CE1 B:HIS161 2.8 26.4 1.0
CE B:MET207 2.9 30.5 1.0
CG B:HIS161 3.2 29.4 1.0
CB B:CYS200 3.3 30.2 1.0
CB B:CYS196 3.4 36.9 1.0
CG B:MET207 3.6 27.8 1.0
CB B:HIS161 3.6 28.5 1.0
NE2 B:HIS161 4.0 22.9 1.0
O B:GLU198 4.2 30.1 1.0
CD2 B:HIS161 4.2 17.4 1.0
CA B:HIS161 4.3 20.5 1.0
ND1 B:HIS204 4.4 24.7 1.0
O B:HIS102 4.5 31.1 1.0
O B:LEU160 4.6 27.2 1.0
CA B:CYS200 4.7 35.9 1.0
CD1 B:TRP104 4.8 19.6 1.0
CA B:CYS196 4.8 29.5 1.0
O B:HIS204 4.9 27.5 1.0
CA B:HIS204 4.9 26.8 1.0
CB B:MET207 4.9 21.6 1.0
CZ2 B:TRP106 5.0 23.6 1.0

Copper binding site 3 out of 6 in 7xma

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Copper binding site 3 out of 6 in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu601

b:20.1
occ:1.00
CU2 B:CUA601 0.0 20.1 1.0
ND1 B:HIS204 2.0 24.7 1.0
SG B:CYS200 2.3 26.3 1.0
SG B:CYS196 2.3 23.6 1.0
CU1 B:CUA601 2.5 17.9 1.0
O B:GLU198 2.6 30.1 1.0
CE1 B:HIS204 2.8 44.1 1.0
CG B:HIS204 3.2 44.8 1.0
CB B:CYS196 3.3 36.9 1.0
CB B:CYS200 3.4 30.2 1.0
O B:HIS204 3.6 27.5 1.0
C B:GLU198 3.6 34.8 1.0
CA B:HIS204 3.7 26.8 1.0
CB B:HIS204 3.7 14.6 1.0
N B:CYS200 3.7 35.2 1.0
NE2 B:HIS204 4.0 30.3 1.0
C B:HIS204 4.1 27.7 1.0
ND1 B:HIS161 4.1 23.7 1.0
SD B:MET207 4.1 30.6 1.0
CD2 B:HIS204 4.2 25.7 1.0
CA B:CYS200 4.2 35.9 1.0
N B:GLU198 4.2 24.9 1.0
C B:ILE199 4.3 32.8 1.0
C B:CYS196 4.3 35.1 1.0
O B:CYS196 4.4 19.9 1.0
CA B:ILE199 4.4 31.1 1.0
CA B:CYS196 4.4 29.5 1.0
N B:ILE199 4.5 22.8 1.0
CA B:GLU198 4.6 28.6 1.0
CG B:MET207 4.6 27.8 1.0
N B:SER197 4.8 25.4 1.0
CE1 B:HIS161 4.9 26.4 1.0
N B:HIS204 4.9 30.5 1.0

Copper binding site 4 out of 6 in 7xma

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Copper binding site 4 out of 6 in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Cu603

b:18.9
occ:1.00
NE2 N:HIS290 2.0 36.5 1.0
NE2 N:HIS291 2.0 25.0 1.0
ND1 N:HIS240 2.3 33.4 1.0
O2 N:PER606 2.3 46.7 1.0
O1 N:PER606 2.4 38.3 1.0
CE1 N:HIS290 2.9 31.3 1.0
CE1 N:HIS291 2.9 28.6 1.0
CD2 N:HIS291 3.0 26.6 1.0
CD2 N:HIS290 3.1 28.2 1.0
CG N:HIS240 3.1 46.5 1.0
CE1 N:HIS240 3.3 37.3 1.0
CB N:HIS240 3.3 24.9 1.0
CA N:HIS240 4.0 45.3 1.0
ND1 N:HIS291 4.0 36.0 1.0
CG N:HIS291 4.0 25.6 1.0
ND1 N:HIS290 4.1 34.1 1.0
CG N:HIS290 4.2 27.9 1.0
CD2 N:HIS240 4.3 17.7 1.0
NE2 N:HIS240 4.4 35.6 1.0
NA N:HEA602 4.5 27.9 1.0
C1A N:HEA602 4.6 26.9 1.0
C4A N:HEA602 4.7 30.7 1.0
N N:HIS240 4.7 17.7 1.0
CG2 N:VAL243 4.9 23.8 1.0
FE N:HEA602 4.9 24.0 1.0
O N:HOH915 4.9 82.7 1.0
C2A N:HEA602 5.0 31.6 1.0
CHA N:HEA602 5.0 18.5 1.0
ND N:HEA602 5.0 26.4 1.0

Copper binding site 5 out of 6 in 7xma

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Copper binding site 5 out of 6 in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Cu601

b:20.4
occ:1.00
CU1 O:CUA601 0.0 20.4 1.0
ND1 O:HIS161 2.0 19.8 1.0
SG O:CYS200 2.3 31.7 1.0
SG O:CYS196 2.3 29.3 1.0
SD O:MET207 2.4 35.9 1.0
CU2 O:CUA601 2.4 20.2 1.0
CE1 O:HIS161 2.8 34.0 1.0
CE O:MET207 3.0 28.4 1.0
CG O:HIS161 3.2 35.5 1.0
CB O:CYS200 3.4 43.6 1.0
CB O:CYS196 3.5 42.1 1.0
CG O:MET207 3.6 32.6 1.0
CB O:HIS161 3.6 39.2 1.0
NE2 O:HIS161 4.0 32.2 1.0
O O:GLU198 4.2 43.5 1.0
CD2 O:HIS161 4.2 20.2 1.0
CA O:HIS161 4.3 35.1 1.0
ND1 O:HIS204 4.4 17.2 1.0
O O:HIS102 4.5 24.9 1.0
O O:LEU160 4.6 30.9 1.0
CD1 O:TRP104 4.8 22.9 1.0
CA O:CYS200 4.8 32.5 1.0
CA O:CYS196 4.9 44.1 1.0
O O:HIS204 4.9 35.8 1.0
CA O:HIS204 4.9 38.4 1.0
CB O:MET207 4.9 32.5 1.0

Copper binding site 6 out of 6 in 7xma

Go back to Copper Binding Sites List in 7xma
Copper binding site 6 out of 6 in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of Bovine Heart Cytochrome C Oxidase, Apo Structure with Dmso within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Cu601

b:20.2
occ:1.00
CU2 O:CUA601 0.0 20.2 1.0
ND1 O:HIS204 2.0 17.2 1.0
SG O:CYS200 2.3 31.7 1.0
SG O:CYS196 2.3 29.3 1.0
CU1 O:CUA601 2.4 20.4 1.0
O O:GLU198 2.6 43.5 1.0
CE1 O:HIS204 2.8 58.1 1.0
CG O:HIS204 3.1 48.4 1.0
CB O:CYS196 3.3 42.1 1.0
CB O:CYS200 3.4 43.6 1.0
O O:HIS204 3.6 35.8 1.0
CA O:HIS204 3.6 38.4 1.0
C O:GLU198 3.6 39.2 1.0
CB O:HIS204 3.7 41.2 1.0
N O:CYS200 3.7 37.8 1.0
NE2 O:HIS204 4.0 22.9 1.0
C O:HIS204 4.1 36.2 1.0
ND1 O:HIS161 4.1 19.8 1.0
SD O:MET207 4.2 35.9 1.0
CD2 O:HIS204 4.2 30.7 1.0
CA O:CYS200 4.2 32.5 1.0
N O:GLU198 4.2 27.2 1.0
C O:ILE199 4.3 32.0 1.0
C O:CYS196 4.3 60.1 1.0
CA O:ILE199 4.4 39.5 1.0
O O:CYS196 4.4 34.5 1.0
CA O:CYS196 4.4 44.1 1.0
N O:ILE199 4.4 21.1 1.0
CA O:GLU198 4.6 30.4 1.0
CG O:MET207 4.6 32.6 1.0
N O:SER197 4.8 31.6 1.0
CE1 O:HIS161 4.9 34.0 1.0
N O:HIS204 4.9 41.7 1.0

Reference:

Y.Nishida, S.Yanagisawa, R.Morita, H.Shigematsu, K.Shinzawa-Itoh, H.Yuki, S.Ogasawara, K.Shimuta, T.Iwamoto, C.Nakabayashi, W.Matsumura, H.Kato, C.Gopalasingam, T.Nagao, T.Qaqorh, Y.Takahashi, S.Yamazaki, K.Kamiya, R.Harada, N.Mizuno, H.Takahashi, Y.Akeda, M.Ohnishi, Y.Ishii, T.Kumasaka, T.Murata, K.Muramoto, T.Tosha, Y.Shiro, T.Honma, Y.Shigeta, M.Kubo, S.Takashima, Y.Shintani. Identifying Antibiotics Based on Structural Differences in the Conserved Allostery From Mitochondrial Heme-Copper Oxidases. Nat Commun V. 13 7591 2022.
ISSN: ESSN 2041-1723
PubMed: 36481732
DOI: 10.1038/S41467-022-34771-Y
Page generated: Wed Jul 31 09:22:31 2024

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