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Copper in PDB 8ji8: Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti

Protein crystallography data

The structure of Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti, PDB code: 8ji8 was solved by X.Zhu, L.Zhang, X.Yang, P.Bao, D.Ren, Q.Han, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.69 / 2.65
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 91.57, 153.66, 223.17, 90, 90, 90
R / Rfree (%) 17.6 / 26.1

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti (pdb code 8ji8). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 8 binding sites of Copper where determined in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti, PDB code: 8ji8:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Copper binding site 1 out of 8 in 8ji8

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Copper binding site 1 out of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti


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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:118.1
occ:1.00
NE2 A:HIS402 2.0 51.1 1.0
NE2 A:HIS366 2.1 47.2 1.0
NE2 A:HIS362 2.1 47.5 1.0
CD2 A:HIS366 2.7 37.7 1.0
CE1 A:HIS402 2.8 46.4 1.0
CD2 A:HIS362 2.8 38.7 1.0
CE1 A:HIS362 3.2 38.9 1.0
CD2 A:HIS402 3.2 40.6 1.0
CE1 A:HIS366 3.2 39.4 1.0
CG A:HIS366 3.9 37.2 1.0
ND1 A:HIS402 4.0 43.5 1.0
CG A:HIS362 4.0 38.1 1.0
ND1 A:HIS362 4.1 39.6 1.0
ND1 A:HIS366 4.1 38.5 1.0
CG A:HIS402 4.2 38.0 1.0
CE2 A:PHE398 4.3 22.6 1.0
NE2 A:HIS235 4.3 87.9 1.0
CZ A:PHE82 4.4 28.4 1.0
CE1 A:PHE82 4.5 27.3 1.0
CD1 A:TRP401 4.6 27.6 1.0
CD2 A:HIS235 4.6 59.8 1.0
CU A:CU702 4.7 171.0 1.0
CZ A:PHE398 4.7 22.7 1.0
NE1 A:TRP401 4.8 28.9 1.0
O A:HIS362 4.9 35.4 1.0
CD2 A:PHE398 4.9 24.2 1.0
CE1 A:HIS235 4.9 77.7 1.0

Copper binding site 2 out of 8 in 8ji8

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Copper binding site 2 out of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti


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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu702

b:171.0
occ:1.00
NE2 A:HIS206 2.1 66.2 1.0
NE2 A:HIS210 2.2 69.4 1.0
NE2 A:HIS235 2.2 87.9 1.0
CD2 A:HIS206 2.9 52.5 1.0
CE1 A:HIS235 2.9 77.7 1.0
CE1 A:HIS206 3.2 50.0 1.0
CE1 A:HIS210 3.2 56.5 1.0
CD2 A:HIS210 3.3 50.6 1.0
CD2 A:HIS235 3.5 59.8 1.0
CG A:HIS206 4.1 45.7 1.0
ND1 A:HIS206 4.1 45.7 1.0
ND1 A:HIS235 4.2 60.3 1.0
CE A:MET234 4.3 51.0 1.0
ND1 A:HIS210 4.4 40.1 1.0
CG A:HIS210 4.5 41.7 1.0
CG A:HIS235 4.5 47.6 1.0
CE1 A:HIS362 4.6 38.9 1.0
NE2 A:HIS362 4.6 47.5 1.0
CU A:CU701 4.7 118.1 1.0
CE3 A:TRP209 4.7 32.1 1.0

Copper binding site 3 out of 8 in 8ji8

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Copper binding site 3 out of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti


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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:116.2
occ:1.00
NE2 B:HIS402 2.1 54.0 1.0
NE2 B:HIS366 2.1 41.0 1.0
NE2 B:HIS362 2.1 47.5 1.0
CE1 B:HIS402 2.8 52.1 1.0
CD2 B:HIS366 2.8 33.6 1.0
CD2 B:HIS362 3.0 36.3 1.0
CE1 B:HIS366 3.1 34.5 1.0
CE1 B:HIS362 3.2 41.1 1.0
CD2 B:HIS402 3.3 43.6 1.0
CG B:HIS366 3.9 33.8 1.0
ND1 B:HIS402 4.0 47.8 1.0
CE2 B:PHE398 4.0 25.2 1.0
ND1 B:HIS366 4.1 34.0 1.0
CG B:HIS362 4.1 36.6 1.0
ND1 B:HIS362 4.2 40.6 1.0
NE2 B:HIS235 4.2 63.7 1.0
CE1 B:PHE82 4.2 27.3 1.0
CG B:HIS402 4.3 42.5 1.0
CU B:CU702 4.4 164.1 1.0
CZ B:PHE82 4.4 28.0 1.0
CD2 B:HIS235 4.6 43.1 1.0
CZ B:PHE398 4.6 24.1 1.0
CD2 B:PHE398 4.7 27.4 1.0
CD1 B:TRP401 4.8 31.4 1.0
CE1 B:HIS206 5.0 46.0 1.0

Copper binding site 4 out of 8 in 8ji8

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Copper binding site 4 out of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti


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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu702

b:164.1
occ:1.00
NE2 B:HIS206 2.1 61.9 1.0
NE2 B:HIS210 2.2 73.9 1.0
NE2 B:HIS235 2.2 63.7 1.0
CE1 B:HIS235 2.9 53.9 1.0
CE1 B:HIS206 3.0 46.0 1.0
CD2 B:HIS206 3.1 49.1 1.0
CE1 B:HIS210 3.1 61.5 1.0
CD2 B:HIS210 3.3 49.5 1.0
CD2 B:HIS235 3.5 43.1 1.0
CE B:MET234 3.9 51.1 1.0
ND1 B:HIS206 4.1 40.8 1.0
CG B:HIS206 4.1 41.1 1.0
ND1 B:HIS235 4.1 41.7 1.0
ND1 B:HIS210 4.3 42.2 1.0
CU B:CU701 4.4 116.2 1.0
CG B:HIS210 4.5 41.0 1.0
CG B:HIS235 4.5 40.4 1.0
CE1 B:HIS362 4.6 41.1 1.0
NE2 B:HIS362 4.6 47.5 1.0
CE2 B:PHE231 4.7 37.0 1.0
SD B:MET234 5.0 55.3 1.0

Copper binding site 5 out of 8 in 8ji8

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Copper binding site 5 out of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti


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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu701

b:128.4
occ:1.00
NE2 C:HIS402 2.1 57.9 1.0
NE2 C:HIS366 2.1 49.4 1.0
NE2 C:HIS362 2.1 43.4 1.0
CE1 C:HIS402 2.7 48.0 1.0
CD2 C:HIS366 2.8 42.9 1.0
CD2 C:HIS362 2.9 36.0 1.0
CE1 C:HIS362 3.2 34.5 1.0
CE1 C:HIS366 3.2 40.2 1.0
CD2 C:HIS402 3.3 42.6 1.0
CG C:HIS366 4.0 42.3 1.0
ND1 C:HIS402 4.0 46.8 1.0
CG C:HIS362 4.0 34.5 1.0
ND1 C:HIS366 4.1 38.0 1.0
ND1 C:HIS362 4.1 36.3 1.0
CE2 C:PHE398 4.2 28.8 1.0
CZ C:PHE82 4.2 31.1 1.0
CG C:HIS402 4.2 41.1 1.0
CE1 C:PHE82 4.3 32.0 1.0
NE2 C:HIS235 4.3 64.6 1.0
CU C:CU702 4.4 157.1 1.0
CZ C:PHE398 4.6 28.0 1.0
CD2 C:HIS235 4.7 46.9 1.0
CD1 C:TRP401 4.8 33.8 1.0
CD2 C:PHE398 4.9 29.7 1.0
O C:HIS362 4.9 36.8 1.0
CE1 C:HIS235 5.0 58.5 1.0

Copper binding site 6 out of 8 in 8ji8

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Copper binding site 6 out of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti


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 Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu702

b:157.1
occ:1.00
NE2 C:HIS206 2.1 62.0 1.0
NE2 C:HIS235 2.2 64.6 1.0
NE2 C:HIS210 2.2 67.0 1.0
CE1 C:HIS235 2.9 58.5 1.0
CD2 C:HIS206 3.0 48.2 1.0
CE1 C:HIS210 3.1 52.8 1.0
CE1 C:HIS206 3.1 54.4 1.0
CD2 C:HIS210 3.3 51.5 1.0
CD2 C:HIS235 3.4 46.9 1.0
CE C:MET234 4.0 50.2 1.0
CG C:HIS206 4.1 44.0 1.0
ND1 C:HIS235 4.2 51.0 1.0
ND1 C:HIS206 4.2 45.4 1.0
ND1 C:HIS210 4.3 44.9 1.0
CU C:CU701 4.4 128.4 1.0
CG C:HIS210 4.5 43.2 1.0
CG C:HIS235 4.5 43.7 1.0
NE2 C:HIS362 4.7 43.4 1.0
CE1 C:HIS362 4.9 34.5 1.0
CE3 C:TRP209 4.9 38.0 1.0

Copper binding site 7 out of 8 in 8ji8

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Copper binding site 7 out of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu701

b:183.8
occ:1.00
NE2 D:HIS206 2.1 60.7 1.0
NE2 D:HIS210 2.2 84.1 1.0
NE2 D:HIS235 2.2 67.2 1.0
CE1 D:HIS235 2.8 52.4 1.0
CE1 D:HIS206 3.0 46.4 1.0
CD2 D:HIS206 3.1 46.0 1.0
CE1 D:HIS210 3.2 68.0 1.0
CD2 D:HIS210 3.3 60.5 1.0
CD2 D:HIS235 3.5 44.8 1.0
ND1 D:HIS206 4.0 43.1 1.0
CE D:MET234 4.1 46.6 1.0
ND1 D:HIS235 4.1 46.5 1.0
CG D:HIS206 4.1 41.0 1.0
CU D:CU702 4.3 131.5 1.0
ND1 D:HIS210 4.3 55.4 1.0
CG D:HIS210 4.4 53.1 1.0
CG D:HIS235 4.5 42.8 1.0
NE2 D:HIS362 4.6 47.2 1.0
CE1 D:HIS362 4.8 38.6 1.0
SD D:MET234 4.9 43.7 1.0
CZ D:PHE398 5.0 26.8 1.0

Copper binding site 8 out of 8 in 8ji8

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Copper binding site 8 out of 8 in the Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Crystal Structure of Prophenoloxidase PPO6 Chimeric Mutant (F215EASNRAIVD224 to G215DGPDSVVR223) From Aedes Aegypti within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu702

b:131.5
occ:1.00
NE2 D:HIS402 2.1 45.9 1.0
NE2 D:HIS366 2.1 45.9 1.0
NE2 D:HIS362 2.1 47.2 1.0
CE1 D:HIS402 2.7 41.2 1.0
CD2 D:HIS366 2.8 40.5 1.0
CD2 D:HIS362 2.9 35.8 1.0
CE1 D:HIS362 3.1 38.6 1.0
CE1 D:HIS366 3.3 36.5 1.0
CD2 D:HIS402 3.3 34.6 1.0
ND1 D:HIS402 4.0 40.8 1.0
CG D:HIS366 4.0 38.8 1.0
CG D:HIS362 4.0 35.3 1.0
NE2 D:HIS235 4.1 67.2 1.0
CE2 D:PHE398 4.1 25.9 1.0
ND1 D:HIS362 4.1 37.1 1.0
ND1 D:HIS366 4.2 37.9 1.0
CG D:HIS402 4.2 34.9 1.0
CU D:CU701 4.3 183.8 1.0
CZ D:PHE82 4.5 27.7 1.0
CD2 D:HIS235 4.5 44.8 1.0
CE1 D:PHE82 4.5 30.6 1.0
CZ D:PHE398 4.6 26.8 1.0
CE1 D:HIS235 4.7 52.4 1.0
CD1 D:TRP401 4.7 29.6 1.0
CD2 D:PHE398 4.8 24.4 1.0
O D:HIS362 4.9 31.4 1.0
NE1 D:TRP401 4.9 27.8 1.0
NE2 D:HIS206 5.0 60.7 1.0

Reference:

X.Zhu, L.Zhang, H.Chen, Y.Tang, L.Jiang, H.Ding, X.Yang, P.Bao, C.Liao, J.Li, D.Ren, C.J.Vavricka, M.R.Strand, Q.Han. Mosquitoes Have Evolved Two Types of Prophenoloxidases To Be Published.
Page generated: Wed Jul 31 09:49:46 2024

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