Copper in PDB 6wje: Copper Resistance Protein Copg- Form 2

Protein crystallography data

The structure of Copper Resistance Protein Copg- Form 2, PDB code: 6wje was solved by A.C.Hausrath, A.T.Ly, M.M.Mcevoy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.42 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.700, 87.460, 143.270, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 24.5

Other elements in 6wje:

The structure of Copper Resistance Protein Copg- Form 2 also contains other interesting chemical elements:

Zinc (Zn) 35 atoms

Copper Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20;

Binding sites:

The binding sites of Copper atom in the Copper Resistance Protein Copg- Form 2 (pdb code 6wje). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 20 binding sites of Copper where determined in the Copper Resistance Protein Copg- Form 2, PDB code: 6wje:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Copper binding site 1 out of 20 in 6wje

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Copper binding site 1 out of 20 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Copper Resistance Protein Copg- Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:43.5
occ:1.00
ND1 A:HIS55 2.1 39.3 1.0
SG A:CYS54 2.1 40.7 1.0
SG A:CYS16 2.2 49.6 1.0
CU A:CU202 2.8 38.5 1.0
CG A:HIS55 2.9 43.6 1.0
CB A:CYS54 2.9 40.9 1.0
CB A:HIS55 3.1 37.1 1.0
CE1 A:HIS55 3.2 43.5 1.0
N A:HIS55 3.3 39.6 1.0
C A:CYS54 3.3 44.6 1.0
CB A:CYS16 3.4 40.0 1.0
NE2 A:HIS67 3.5 34.5 1.0
CA A:CYS54 3.6 40.4 1.0
CA A:CYS16 3.7 46.9 1.0
O A:CYS54 3.7 54.0 1.0
SG A:CYS13 3.7 64.0 1.0
CA A:HIS55 3.8 36.1 1.0
N A:CYS16 4.1 42.8 1.0
CD2 A:HIS55 4.1 40.5 1.0
CD2 A:HIS67 4.1 31.4 1.0
NE2 A:HIS55 4.2 39.9 1.0
N A:CYS54 4.3 40.0 1.0
CE1 A:HIS67 4.3 36.6 1.0
SG A:CYS15 4.5 40.9 1.0
C A:HIS55 4.9 44.7 1.0
C A:CYS15 4.9 38.4 1.0

Copper binding site 2 out of 20 in 6wje

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Copper binding site 2 out of 20 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Copper Resistance Protein Copg- Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu202

b:38.5
occ:1.00
NE2 A:HIS67 2.1 34.5 1.0
SG A:CYS54 2.2 40.7 1.0
SG A:CYS15 2.2 40.9 1.0
CU A:CU201 2.8 43.5 1.0
CE1 A:HIS67 3.0 36.6 1.0
CD2 A:HIS67 3.1 31.4 1.0
CU A:CU203 3.2 48.1 1.0
CB A:CYS15 3.3 33.8 1.0
CB A:CYS54 3.4 40.9 1.0
SD A:MET90 3.5 46.1 1.0
SG A:CYS16 3.7 49.6 1.0
N A:CYS16 3.8 42.8 1.0
SG A:CYS13 3.9 64.0 1.0
CG A:MET90 3.9 41.9 1.0
C A:CYS15 4.0 38.4 1.0
ND1 A:HIS67 4.1 32.9 1.0
CG A:HIS67 4.2 35.8 1.0
CA A:CYS15 4.2 37.7 1.0
CA A:CYS16 4.3 46.9 1.0
CG A:MET97 4.3 35.1 1.0
ND1 A:HIS55 4.4 39.3 1.0
SD A:MET97 4.5 45.0 1.0
O A:CYS15 4.7 37.2 1.0
CB A:CYS16 4.7 40.0 1.0
CA A:CYS54 4.7 40.4 1.0
CE1 A:HIS55 4.9 43.5 1.0

Copper binding site 3 out of 20 in 6wje

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Copper binding site 3 out of 20 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Copper Resistance Protein Copg- Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu203

b:48.1
occ:1.00
SD A:MET97 2.3 45.0 1.0
SG A:CYS15 2.4 40.9 1.0
SD A:MET90 2.4 46.1 1.0
SD B:MET99 2.6 44.8 1.0
CE A:MET90 2.9 41.6 1.0
CB A:CYS15 3.2 33.8 1.0
CG B:MET99 3.2 32.5 1.0
CU A:CU202 3.2 38.5 1.0
CE B:MET99 3.3 48.3 1.0
CE A:MET97 3.4 34.1 1.0
CG A:MET90 3.4 41.9 1.0
CG A:MET97 3.5 35.1 1.0
CB A:MET90 3.8 36.1 1.0
CB B:MET99 3.9 30.2 1.0
NE2 A:HIS67 4.4 34.5 1.0
CA A:CYS15 4.6 37.7 1.0
SG A:CYS54 4.7 40.7 1.0
CB A:MET97 4.9 37.1 1.0

Copper binding site 4 out of 20 in 6wje

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Copper binding site 4 out of 20 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Copper Resistance Protein Copg- Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu201

b:50.3
occ:1.00
ND1 B:HIS55 2.1 42.8 1.0
SG B:CYS54 2.3 42.7 1.0
SG B:CYS16 2.3 51.3 1.0
CU B:CU202 2.8 44.3 1.0
CB B:CYS54 2.9 41.1 1.0
CG B:HIS55 3.0 48.5 1.0
CE1 B:HIS55 3.1 42.5 1.0
CB B:HIS55 3.2 43.3 1.0
C B:CYS54 3.3 42.8 1.0
N B:HIS55 3.4 44.1 1.0
CB B:CYS16 3.4 41.4 1.0
NE2 B:HIS67 3.5 34.2 1.0
CA B:CYS54 3.6 38.1 1.0
CA B:CYS16 3.7 44.6 1.0
O B:CYS54 3.8 52.8 1.0
SG B:CYS13 3.8 72.5 1.0
CA B:HIS55 3.9 41.8 1.0
N B:CYS16 4.1 46.0 1.0
CD2 B:HIS55 4.1 38.6 1.0
N B:CYS54 4.1 40.0 1.0
CD2 B:HIS67 4.1 30.7 1.0
NE2 B:HIS55 4.1 47.5 1.0
CE1 B:HIS67 4.2 40.8 1.0
SG B:CYS15 4.3 46.7 1.0
C B:CYS15 4.8 46.4 1.0
O B:HOH302 5.0 50.2 1.0
C B:HIS55 5.0 45.0 1.0

Copper binding site 5 out of 20 in 6wje

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Copper binding site 5 out of 20 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Copper Resistance Protein Copg- Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu202

b:44.3
occ:1.00
NE2 B:HIS67 2.1 34.2 1.0
SG B:CYS15 2.2 46.7 1.0
SG B:CYS54 2.3 42.7 1.0
CU B:CU201 2.8 50.3 1.0
CE1 B:HIS67 3.0 40.8 1.0
CD2 B:HIS67 3.1 30.7 1.0
CB B:CYS15 3.2 42.5 1.0
CU B:CU203 3.2 48.9 1.0
CB B:CYS54 3.4 41.1 1.0
CG B:MET90 3.7 44.3 1.0
SD B:MET90 3.7 52.5 1.0
N B:CYS16 3.8 46.0 1.0
SG B:CYS16 3.8 51.3 1.0
C B:CYS15 3.9 46.4 1.0
SG B:CYS13 4.1 72.5 1.0
CA B:CYS15 4.1 44.3 1.0
ND1 B:HIS67 4.1 41.2 1.0
CG B:HIS67 4.2 38.8 1.0
CG B:MET97 4.3 35.2 1.0
ND1 B:HIS55 4.3 42.8 1.0
CA B:CYS16 4.4 44.6 1.0
O B:CYS15 4.4 42.4 1.0
SD B:MET97 4.6 40.5 1.0
CB B:CYS16 4.7 41.4 1.0
CE1 B:HIS55 4.7 42.5 1.0
CA B:CYS54 4.8 38.1 1.0
CB B:MET90 5.0 38.1 1.0

Copper binding site 6 out of 20 in 6wje

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Copper binding site 6 out of 20 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Copper Resistance Protein Copg- Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu203

b:48.9
occ:1.00
SG B:CYS15 2.4 46.7 1.0
SD B:MET90 2.4 52.5 1.0
SD B:MET97 2.5 40.5 1.0
SD A:MET99 2.7 49.0 1.0
CB B:CYS15 2.8 42.5 1.0
CG A:MET99 3.0 48.6 1.0
CU B:CU202 3.2 44.3 1.0
CG B:MET90 3.3 44.3 1.0
CE B:MET97 3.5 38.0 1.0
CG B:MET97 3.5 35.2 1.0
CE B:MET90 3.6 51.5 1.0
CE A:MET99 3.7 52.4 1.0
CB B:MET90 3.9 38.1 1.0
CB A:MET99 4.1 48.4 1.0
CA B:CYS15 4.4 44.3 1.0
NE2 B:HIS67 4.4 34.2 1.0
SG B:CYS54 4.7 42.7 1.0
CB B:MET97 4.9 34.7 1.0
N B:CYS15 4.9 44.8 1.0

Copper binding site 7 out of 20 in 6wje

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Copper binding site 7 out of 20 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Copper Resistance Protein Copg- Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu201

b:48.0
occ:1.00
ND1 C:HIS55 2.1 39.4 1.0
SG C:CYS16 2.1 42.1 0.6
SG C:CYS54 2.2 39.2 1.0
SG C:CYS16 2.3 42.3 0.4
CU C:CU203 2.8 48.5 0.6
CU C:CU202 2.8 46.6 1.0
CG C:HIS55 2.9 42.7 1.0
CB C:CYS54 2.9 44.0 1.0
CB C:HIS55 3.1 35.6 1.0
CE1 C:HIS55 3.1 39.3 1.0
CB C:CYS16 3.3 45.0 0.6
C C:CYS54 3.3 43.6 1.0
N C:HIS55 3.4 42.7 1.0
CB C:CYS16 3.4 45.0 0.4
CA C:CYS16 3.6 42.1 0.6
CA C:CYS16 3.6 42.1 0.4
CA C:CYS54 3.6 39.6 1.0
O C:CYS54 3.7 51.9 1.0
NE2 C:HIS67 3.8 33.3 1.0
CA C:HIS55 3.8 42.9 1.0
SG C:CYS13 3.8 53.8 0.4
N C:CYS16 4.0 43.4 0.6
N C:CYS16 4.0 43.4 0.4
CD2 C:HIS55 4.1 40.0 1.0
NE2 C:HIS55 4.2 42.4 1.0
SG C:CYS15 4.3 40.1 1.0
N C:CYS54 4.3 43.5 1.0
CD2 C:HIS67 4.4 39.2 1.0
CE1 C:HIS67 4.4 36.4 1.0
SG C:CYS13 4.6 64.3 0.6
C C:CYS15 4.7 45.3 1.0
C C:HIS55 4.9 42.9 1.0
C C:CYS16 5.0 45.2 0.4
C C:CYS16 5.0 45.3 0.6

Copper binding site 8 out of 20 in 6wje

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Copper binding site 8 out of 20 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Copper Resistance Protein Copg- Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu202

b:46.6
occ:1.00
NE2 C:HIS67 2.0 33.3 1.0
SG C:CYS54 2.2 39.2 1.0
SG C:CYS15 2.2 40.1 1.0
CU C:CU203 2.7 48.5 0.6
CU C:CU201 2.8 48.0 1.0
CE1 C:HIS67 2.9 36.4 1.0
CU C:CU204 3.1 46.5 1.0
CD2 C:HIS67 3.1 39.2 1.0
CB C:CYS15 3.3 42.8 1.0
CB C:CYS54 3.3 44.0 1.0
SD C:MET90 3.7 55.4 1.0
N C:CYS16 3.9 43.4 0.6
N C:CYS16 3.9 43.4 0.4
C C:CYS15 4.0 45.3 1.0
SG C:CYS16 4.0 42.1 0.6
ND1 C:HIS67 4.1 35.5 1.0
CG C:MET90 4.2 42.5 1.0
CG C:HIS67 4.2 43.5 1.0
CA C:CYS15 4.2 37.6 1.0
SG C:CYS16 4.2 42.3 0.4
OD2 D:OMT99 4.3 53.0 1.0
CG C:MET97 4.3 40.8 1.0
ND1 C:HIS55 4.3 39.4 1.0
O C:CYS15 4.4 49.4 1.0
CA C:CYS16 4.4 42.1 0.6
CA C:CYS16 4.4 42.1 0.4
SD C:MET97 4.5 54.3 1.0
OD1 D:OMT99 4.6 57.2 1.0
CA C:CYS54 4.7 39.6 1.0
CE1 C:HIS55 4.7 39.3 1.0
SG C:CYS13 4.8 53.8 0.4
CB C:CYS16 4.9 45.0 0.6
CB C:CYS16 5.0 45.0 0.4

Copper binding site 9 out of 20 in 6wje

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Copper binding site 9 out of 20 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 9 of Copper Resistance Protein Copg- Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu203

b:48.5
occ:0.58
SG C:CYS13 2.2 53.8 0.4
SG C:CYS15 2.2 40.1 1.0
SG C:CYS16 2.2 42.1 0.6
SG C:CYS16 2.4 42.3 0.4
N C:CYS16 2.7 43.4 0.4
N C:CYS16 2.7 43.4 0.6
CU C:CU202 2.7 46.6 1.0
OD1 D:OMT99 2.8 57.2 1.0
CU C:CU201 2.8 48.0 1.0
SG C:CYS13 2.9 64.3 0.6
CB C:CYS16 3.1 45.0 0.6
CB C:CYS16 3.2 45.0 0.4
CA C:CYS16 3.3 42.1 0.4
CA C:CYS16 3.3 42.1 0.6
CB C:CYS13 3.4 45.0 0.6
CB C:CYS54 3.4 44.0 1.0
C C:CYS15 3.5 45.3 1.0
SG C:CYS54 3.5 39.2 1.0
CB C:CYS15 3.6 42.8 1.0
CB C:CYS13 3.7 44.4 0.4
SD D:OMT99 3.8 81.1 1.0
CA C:CYS15 3.8 37.6 1.0
OD2 D:OMT99 3.9 53.0 1.0
N C:CYS15 4.0 43.6 1.0
CA C:CYS13 4.1 49.0 0.6
CA C:CYS13 4.1 49.0 0.4
C C:CYS13 4.1 48.7 0.4
C C:CYS13 4.1 48.7 0.6
O C:CYS13 4.2 51.2 0.4
O C:CYS13 4.3 51.3 0.6
CU C:CU204 4.4 46.5 1.0
O C:CYS15 4.5 49.4 1.0
NE2 C:HIS67 4.5 33.3 1.0
N C:GLY14 4.6 40.8 1.0
ND1 C:HIS55 4.7 39.4 1.0
CE D:OMT99 4.7 43.7 1.0
CA C:CYS54 4.7 39.6 1.0
C C:GLY14 4.7 43.7 1.0
C C:CYS16 4.8 45.2 0.4
C C:CYS16 4.8 45.3 0.6
O C:CYS54 4.8 51.9 1.0
C C:CYS54 4.9 43.6 1.0
CE1 C:HIS67 4.9 36.4 1.0

Copper binding site 10 out of 20 in 6wje

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Copper binding site 10 out of 20 in the Copper Resistance Protein Copg- Form 2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 10 of Copper Resistance Protein Copg- Form 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu204

b:46.5
occ:1.00
SD C:MET97 2.4 54.3 1.0
SG C:CYS15 2.4 40.1 1.0
SD C:MET90 2.4 55.4 1.0
O D:HOH301 2.5 38.5 1.0
OD2 D:OMT99 2.5 53.0 1.0
CB C:CYS15 3.1 42.8 1.0
CU C:CU202 3.1 46.6 1.0
CE C:MET90 3.2 47.4 1.0
CG C:MET97 3.4 40.8 1.0
CG C:MET90 3.5 42.5 1.0
CE C:MET97 3.5 43.0 1.0
SD D:OMT99 3.9 81.1 1.0
CB C:MET90 3.9 49.6 1.0
NE2 C:HIS67 4.1 33.3 1.0
CU C:CU203 4.4 48.5 0.6
OD1 D:OMT99 4.4 57.2 1.0
SG C:CYS54 4.6 39.2 1.0
CA C:CYS15 4.6 37.6 1.0
CE D:OMT99 4.7 43.7 1.0
CE1 C:HIS67 4.7 36.4 1.0
CB C:MET97 4.8 37.4 1.0
CD2 C:HIS67 4.9 39.2 1.0
CG D:OMT99 4.9 61.7 1.0
CB C:CYS54 5.0 44.0 1.0

Reference:

A.C.Hausrath, N.A.Ramirez, A.T.Ly, M.M.Mcevoy. The Bacterial Copper-Resistance Protein Copg Contains A Cysteine-Bridged Tetranuclear Copper Cluster J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
Page generated: Sun Dec 13 11:26:26 2020

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