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Copper in PDB 8c8q: Cytochrome C Oxidase From Schizosaccharomyces Pombe

Enzymatic activity of Cytochrome C Oxidase From Schizosaccharomyces Pombe

All present enzymatic activity of Cytochrome C Oxidase From Schizosaccharomyces Pombe:
7.1.1.9;

Other elements in 8c8q:

The structure of Cytochrome C Oxidase From Schizosaccharomyces Pombe also contains other interesting chemical elements:

Calcium (Ca) 1 atom
Iron (Fe) 2 atoms
Zinc (Zn) 1 atom
Magnesium (Mg) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Cytochrome C Oxidase From Schizosaccharomyces Pombe (pdb code 8c8q). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Cytochrome C Oxidase From Schizosaccharomyces Pombe, PDB code: 8c8q:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 8c8q

Go back to Copper Binding Sites List in 8c8q
Copper binding site 1 out of 3 in the Cytochrome C Oxidase From Schizosaccharomyces Pombe


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cytochrome C Oxidase From Schizosaccharomyces Pombe within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu603

b:86.4
occ:1.00
NE2 A:HIS297 1.9 35.0 1.0
NE2 A:HIS296 2.4 47.0 1.0
CE1 A:HIS296 2.6 48.1 1.0
ND1 A:HIS247 2.6 36.2 1.0
CE1 A:HIS297 2.7 39.6 1.0
CD2 A:HIS297 3.0 35.8 1.0
CE1 A:HIS247 3.3 37.1 1.0
CD2 A:HIS296 3.6 37.8 1.0
CG A:HIS247 3.8 37.7 1.0
ND1 A:HIS296 3.8 37.6 1.0
ND1 A:HIS297 3.8 35.9 1.0
CG A:HIS297 4.0 33.9 1.0
CB A:HIS247 4.2 32.6 1.0
CG A:HIS296 4.3 29.9 1.0
C1A A:HEA602 4.4 37.0 1.0
FE A:HEA602 4.5 54.4 1.0
NA A:HEA602 4.5 43.5 1.0
NE2 A:HIS247 4.5 34.2 1.0
C4A A:HEA602 4.5 42.3 1.0
C2A A:HEA602 4.7 38.2 1.0
CD2 A:HIS247 4.7 32.5 1.0
C3A A:HEA602 4.7 38.3 1.0
CA A:HIS247 4.8 33.5 1.0
ND A:HEA602 4.8 41.3 1.0
CHA A:HEA602 4.9 31.4 1.0
CG2 A:VAL250 4.9 34.0 1.0
C4D A:HEA602 5.0 34.0 1.0

Copper binding site 2 out of 3 in 8c8q

Go back to Copper Binding Sites List in 8c8q
Copper binding site 2 out of 3 in the Cytochrome C Oxidase From Schizosaccharomyces Pombe


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Cytochrome C Oxidase From Schizosaccharomyces Pombe within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu302

b:55.7
occ:1.00
CU1 B:CUA302 0.0 55.7 1.0
ND1 B:HIS182 2.4 40.5 1.0
CU2 B:CUA302 2.7 94.2 1.0
SG B:CYS221 2.8 65.8 1.0
CE1 B:HIS182 2.8 50.2 1.0
SD B:MET228 2.9 47.3 1.0
CE B:MET228 3.0 50.6 1.0
SG B:CYS217 3.2 61.9 1.0
CB B:CYS221 3.5 46.2 1.0
CG B:HIS182 3.7 46.3 1.0
CB B:CYS217 3.8 38.5 1.0
O B:GLU219 3.9 56.3 1.0
NE2 B:HIS182 4.1 53.5 1.0
CG B:MET228 4.3 48.5 1.0
CB B:HIS182 4.3 48.6 1.0
CD2 B:HIS182 4.5 50.2 1.0
ND1 B:HIS225 4.6 32.3 1.0
CB B:MET228 4.6 46.6 1.0
N B:CYS221 4.7 45.4 1.0
CA B:CYS221 4.7 41.0 1.0
CA B:HIS182 4.7 46.2 1.0

Copper binding site 3 out of 3 in 8c8q

Go back to Copper Binding Sites List in 8c8q
Copper binding site 3 out of 3 in the Cytochrome C Oxidase From Schizosaccharomyces Pombe


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Cytochrome C Oxidase From Schizosaccharomyces Pombe within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu302

b:94.2
occ:1.00
CU2 B:CUA302 0.0 94.2 1.0
ND1 B:HIS225 1.9 32.3 1.0
O B:GLU219 2.7 56.3 1.0
CU1 B:CUA302 2.7 55.7 1.0
CE1 B:HIS225 2.8 33.8 1.0
CG B:HIS225 2.8 32.8 1.0
SG B:CYS221 3.2 65.8 1.0
CB B:HIS225 3.3 33.8 1.0
CA B:HIS225 3.4 32.5 1.0
O B:HIS225 3.4 47.7 1.0
C B:GLU219 3.5 48.3 1.0
N B:CYS221 3.6 45.4 1.0
CA B:LEU220 3.6 49.6 1.0
SG B:CYS217 3.7 61.9 1.0
NE2 B:HIS225 3.8 34.5 1.0
CD2 B:HIS225 3.9 37.3 1.0
C B:HIS225 3.9 37.6 1.0
C B:LEU220 3.9 43.5 1.0
N B:LEU220 4.0 47.2 1.0
CB B:CYS217 4.0 38.5 1.0
CB B:CYS221 4.0 46.2 1.0
N B:GLU219 4.4 43.0 1.0
CA B:CYS221 4.5 41.0 1.0
CA B:GLU219 4.6 44.5 1.0
N B:HIS225 4.6 38.7 1.0
O B:CYS217 4.7 58.2 1.0
C B:CYS217 4.8 44.4 1.0
ND1 B:HIS182 4.8 40.5 1.0
O B:LEU220 4.9 37.2 1.0
CB B:LEU220 4.9 39.3 1.0
SD B:MET228 5.0 47.3 1.0

Reference:

A.Moe, P.Adelroth, P.Brzezinski, L.Nasvik Ojemyr. Cryo-Em Structure and Function of S. Pombe Complex IV with Bound Respiratory Supercomplex Factor. Commun Chem V. 6 32 2023.
ISSN: ESSN 2399-3669
PubMed: 36797353
DOI: 10.1038/S42004-023-00827-3
Page generated: Wed Jul 31 09:33:08 2024

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