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Copper in PDB 8sr5: Particulate Methane Monooxygenase Potassium Cyanide Treated

Enzymatic activity of Particulate Methane Monooxygenase Potassium Cyanide Treated

All present enzymatic activity of Particulate Methane Monooxygenase Potassium Cyanide Treated:
1.14.18.3;

Copper Binding Sites:

The binding sites of Copper atom in the Particulate Methane Monooxygenase Potassium Cyanide Treated (pdb code 8sr5). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Particulate Methane Monooxygenase Potassium Cyanide Treated, PDB code: 8sr5:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 8sr5

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Copper binding site 1 out of 6 in the Particulate Methane Monooxygenase Potassium Cyanide Treated


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Particulate Methane Monooxygenase Potassium Cyanide Treated within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:107.6
occ:1.00
 ND1 A:HIS33 1.9 92.3 1.0
NE2 A:HIS139 2.0 74.6 1.0
ND1 A:HIS137 2.2 78.9 1.0
N A:HIS33 2.4 92.3 1.0
CE1 A:HIS137 2.7 78.9 1.0
CE1 A:HIS33 2.8 92.3 1.0
CA A:HIS33 2.9 92.3 1.0
CE1 A:HIS139 2.9 74.6 1.0
CG A:HIS33 3.1 92.3 1.0
CD2 A:HIS139 3.1 74.6 1.0
CG A:HIS137 3.4 78.9 1.0
CB A:HIS33 3.5 92.3 1.0
NE2 A:HIS137 3.8 78.9 1.0
NE2 A:HIS33 4.0 92.3 1.0
CB A:HIS137 4.0 78.9 1.0
ND1 A:HIS139 4.1 74.6 1.0
CD2 A:HIS33 4.1 92.3 1.0
CG A:HIS139 4.1 74.6 1.0
CD2 A:HIS137 4.2 78.9 1.0
C A:HIS33 4.2 92.3 1.0
N A:GLY34 4.7 90.2 1.0

Copper binding site 2 out of 6 in 8sr5

Go back to Copper Binding Sites List in 8sr5
Copper binding site 2 out of 6 in the Particulate Methane Monooxygenase Potassium Cyanide Treated


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Particulate Methane Monooxygenase Potassium Cyanide Treated within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:87.1
occ:1.00
 ND1 A:HIS48 2.0 70.3 1.0
OE1 A:GLN404 2.0 71.4 1.0
ND1 A:HIS72 2.0 70.3 1.0
CE1 A:HIS72 2.6 70.3 1.0
CE1 A:HIS48 2.7 70.3 1.0
CD A:GLN404 3.1 71.4 1.0
CG A:HIS48 3.1 70.3 1.0
CG A:HIS72 3.2 70.3 1.0
O A:HIS72 3.7 70.3 1.0
CB A:HIS48 3.7 70.3 1.0
CD2 A:LEU390 3.8 72.8 1.0
NE2 A:HIS72 3.8 70.3 1.0
NE2 A:GLN404 3.8 71.4 1.0
CB A:HIS72 3.9 70.3 1.0
NE2 A:HIS48 3.9 70.3 1.0
CD1 A:PHE74 4.0 70.3 1.0
CD2 A:HIS48 4.1 70.3 1.0
CA A:PHE74 4.1 70.3 1.0
CD2 A:HIS72 4.1 70.3 1.0
CG A:GLN404 4.2 71.4 1.0
CB A:PHE74 4.3 70.3 1.0
C A:HIS72 4.4 70.3 1.0
CG A:LEU390 4.4 72.8 1.0
N A:PHE74 4.4 70.3 1.0
CG A:PHE74 4.6 70.3 1.0
CD1 A:LEU390 4.7 72.8 1.0
N A:HIS48 4.7 70.3 1.0
CA A:HIS72 4.8 70.3 1.0
C A:VAL73 4.8 70.3 1.0
CA A:HIS48 4.8 70.3 1.0
CE1 A:PHE74 4.9 70.3 1.0
O A:VAL73 5.0 70.3 1.0

Copper binding site 3 out of 6 in 8sr5

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Copper binding site 3 out of 6 in the Particulate Methane Monooxygenase Potassium Cyanide Treated


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Particulate Methane Monooxygenase Potassium Cyanide Treated within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu501

b:107.6
occ:1.00
 ND1 E:HIS33 1.9 92.3 1.0
NE2 E:HIS139 2.0 74.6 1.0
ND1 E:HIS137 2.2 78.9 1.0
N E:HIS33 2.4 92.3 1.0
CE1 E:HIS137 2.7 78.9 1.0
CE1 E:HIS33 2.8 92.3 1.0
CA E:HIS33 2.9 92.3 1.0
CE1 E:HIS139 2.9 74.6 1.0
CG E:HIS33 3.1 92.3 1.0
CD2 E:HIS139 3.1 74.6 1.0
CG E:HIS137 3.4 78.9 1.0
CB E:HIS33 3.5 92.3 1.0
NE2 E:HIS137 3.8 78.9 1.0
NE2 E:HIS33 4.0 92.3 1.0
CB E:HIS137 4.0 78.9 1.0
ND1 E:HIS139 4.1 74.6 1.0
CD2 E:HIS33 4.1 92.3 1.0
CG E:HIS139 4.1 74.6 1.0
CD2 E:HIS137 4.2 78.9 1.0
C E:HIS33 4.2 92.3 1.0
N E:GLY34 4.7 90.2 1.0

Copper binding site 4 out of 6 in 8sr5

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Copper binding site 4 out of 6 in the Particulate Methane Monooxygenase Potassium Cyanide Treated


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Particulate Methane Monooxygenase Potassium Cyanide Treated within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu502

b:87.1
occ:1.00
 ND1 E:HIS48 2.0 70.3 1.0
OE1 E:GLN404 2.0 71.4 1.0
ND1 E:HIS72 2.0 70.3 1.0
CE1 E:HIS72 2.6 70.3 1.0
CE1 E:HIS48 2.7 70.3 1.0
CD E:GLN404 3.1 71.4 1.0
CG E:HIS48 3.1 70.3 1.0
CG E:HIS72 3.2 70.3 1.0
O E:HIS72 3.7 70.3 1.0
CB E:HIS48 3.7 70.3 1.0
CD2 E:LEU390 3.8 72.8 1.0
NE2 E:HIS72 3.8 70.3 1.0
NE2 E:GLN404 3.8 71.4 1.0
CB E:HIS72 3.9 70.3 1.0
NE2 E:HIS48 3.9 70.3 1.0
CD1 E:PHE74 4.0 70.3 1.0
CD2 E:HIS48 4.1 70.3 1.0
CA E:PHE74 4.1 70.3 1.0
CD2 E:HIS72 4.1 70.3 1.0
CG E:GLN404 4.2 71.4 1.0
CB E:PHE74 4.3 70.3 1.0
C E:HIS72 4.4 70.3 1.0
CG E:LEU390 4.4 72.8 1.0
N E:PHE74 4.4 70.3 1.0
CG E:PHE74 4.6 70.3 1.0
CD1 E:LEU390 4.7 72.8 1.0
N E:HIS48 4.7 70.3 1.0
CA E:HIS72 4.8 70.3 1.0
C E:VAL73 4.8 70.3 1.0
CA E:HIS48 4.8 70.3 1.0
CE1 E:PHE74 4.9 70.3 1.0
O E:VAL73 5.0 70.3 1.0

Copper binding site 5 out of 6 in 8sr5

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Copper binding site 5 out of 6 in the Particulate Methane Monooxygenase Potassium Cyanide Treated


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Particulate Methane Monooxygenase Potassium Cyanide Treated within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Cu501

b:107.6
occ:1.00
 ND1 I:HIS33 2.0 92.3 1.0
NE2 I:HIS139 2.0 74.6 1.0
ND1 I:HIS137 2.2 78.9 1.0
N I:HIS33 2.4 92.3 1.0
CE1 I:HIS137 2.7 78.9 1.0
CE1 I:HIS33 2.8 92.3 1.0
CA I:HIS33 2.9 92.3 1.0
CE1 I:HIS139 2.9 74.6 1.0
CG I:HIS33 3.1 92.3 1.0
CD2 I:HIS139 3.1 74.6 1.0
CG I:HIS137 3.4 78.9 1.0
CB I:HIS33 3.5 92.3 1.0
NE2 I:HIS137 3.8 78.9 1.0
NE2 I:HIS33 4.0 92.3 1.0
CB I:HIS137 4.0 78.9 1.0
ND1 I:HIS139 4.1 74.6 1.0
CD2 I:HIS33 4.1 92.3 1.0
CG I:HIS139 4.1 74.6 1.0
CD2 I:HIS137 4.2 78.9 1.0
C I:HIS33 4.2 92.3 1.0
N I:GLY34 4.7 90.2 1.0

Copper binding site 6 out of 6 in 8sr5

Go back to Copper Binding Sites List in 8sr5
Copper binding site 6 out of 6 in the Particulate Methane Monooxygenase Potassium Cyanide Treated


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Particulate Methane Monooxygenase Potassium Cyanide Treated within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Cu502

b:87.1
occ:1.00
 ND1 I:HIS48 2.0 70.3 1.0
OE1 I:GLN404 2.0 71.4 1.0
ND1 I:HIS72 2.0 70.3 1.0
CE1 I:HIS72 2.6 70.3 1.0
CE1 I:HIS48 2.7 70.3 1.0
CD I:GLN404 3.1 71.4 1.0
CG I:HIS48 3.1 70.3 1.0
CG I:HIS72 3.2 70.3 1.0
O I:HIS72 3.7 70.3 1.0
CB I:HIS48 3.7 70.3 1.0
CD2 I:LEU390 3.8 72.8 1.0
NE2 I:HIS72 3.8 70.3 1.0
NE2 I:GLN404 3.8 71.4 1.0
CB I:HIS72 3.9 70.3 1.0
NE2 I:HIS48 3.9 70.3 1.0
CD1 I:PHE74 4.0 70.3 1.0
CD2 I:HIS48 4.1 70.3 1.0
CA I:PHE74 4.1 70.3 1.0
CD2 I:HIS72 4.1 70.3 1.0
CG I:GLN404 4.2 71.4 1.0
CB I:PHE74 4.3 70.3 1.0
C I:HIS72 4.4 70.3 1.0
CG I:LEU390 4.4 72.8 1.0
N I:PHE74 4.4 70.3 1.0
CG I:PHE74 4.6 70.3 1.0
CD1 I:LEU390 4.7 72.8 1.0
N I:HIS48 4.7 70.3 1.0
CA I:HIS72 4.8 70.3 1.0
C I:VAL73 4.8 70.3 1.0
CA I:HIS48 4.8 70.3 1.0
CE1 I:PHE74 4.9 70.3 1.0
O I:VAL73 5.0 70.3 1.0

Reference:

F.J.Tucci, R.J.Jodts, B.M.Hoffman, A.C.Rosenzweig. Product Analogue Binding Identifies the Copper Active Site of Particulate Methane Monooxygenase Nat Catal 2023.
ISSN: ESSN 2520-1158
DOI: 10.1038/S41929-023-01051-X
Page generated: Wed Jul 31 10:18:22 2024

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