Copper in PDB 8jib: Crystal Structure of Prophenoloxidase PPO6 From Aedes Aegypti

The structure of Crystal Structure of Prophenoloxidase PPO6 From Aedes Aegypti, PDB code: 8jib 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)	48.66 / 3.15
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	121.041, 364.149, 125.522, 90, 118.95, 90
R / Rfree (%)	26.9 / 31

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 24;

Binding sites:

The binding sites of Copper atom in the Crystal Structure of Prophenoloxidase PPO6 From Aedes Aegypti (pdb code 8jib). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 24 binding sites of Copper where determined in the Crystal Structure of Prophenoloxidase PPO6 From Aedes Aegypti, PDB code: 8jib:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Copper binding site 1 out of 24 in the Crystal Structure of Prophenoloxidase PPO6 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 From Aedes Aegypti within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu701 b:55.4 occ:1.00 NE2 A:HIS403 2.0 38.6 1.0 NE2 A:HIS367 2.0 38.2 1.0 NE2 A:HIS363 2.0 39.1 1.0 CE1 A:HIS403 2.8 38.3 1.0 CE1 A:HIS367 2.9 35.0 1.0 CE1 A:HIS363 3.0 35.5 1.0 CD2 A:HIS367 3.0 35.6 1.0 CD2 A:HIS363 3.1 36.3 1.0 CD2 A:HIS403 3.2 35.2 1.0 CU A:CU702 3.8 61.7 1.0 CE2 A:PHE399 3.9 40.1 1.0 ND1 A:HIS367 4.0 34.6 1.0 ND1 A:HIS403 4.0 39.4 1.0 CG A:HIS367 4.1 35.0 1.0 ND1 A:HIS363 4.1 35.8 1.0 CG A:HIS363 4.2 36.4 1.0 CG A:HIS403 4.2 36.6 1.0 NE2 A:HIS236 4.3 51.9 1.0 CZ A:PHE82 4.5 41.4 1.0 CZ A:PHE399 4.5 38.6 1.0 CD2 A:HIS236 4.6 47.0 1.0 CD2 A:PHE399 4.7 40.6 1.0 CE1 A:HIS206 4.9 58.4 1.0 NE2 A:HIS206 4.9 58.7 1.0

Copper binding site 2 out of 24 in the Crystal Structure of Prophenoloxidase PPO6 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 From Aedes Aegypti within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu702 b:61.7 occ:1.00 NE2 A:HIS210 2.0 62.1 1.0 NE2 A:HIS206 2.0 58.7 1.0 NE2 A:HIS236 2.1 51.9 1.0 CE1 A:HIS206 2.8 58.4 1.0 CE1 A:HIS236 2.9 50.7 1.0 CE1 A:HIS210 2.9 60.0 1.0 CD2 A:HIS210 3.1 62.3 1.0 CD2 A:HIS206 3.1 54.3 1.0 CD2 A:HIS236 3.2 47.0 1.0 CU A:CU701 3.8 55.4 1.0 ND1 A:HIS206 3.9 52.3 1.0 ND1 A:HIS210 4.1 57.8 1.0 ND1 A:HIS236 4.1 47.6 1.0 CG A:HIS206 4.1 53.3 1.0 CG A:HIS210 4.2 55.4 1.0 CG A:HIS236 4.3 43.9 1.0 NE2 A:HIS403 4.5 38.6 1.0 NE2 A:HIS363 4.6 39.1 1.0 CE1 A:HIS363 4.7 35.5 1.0 CE1 A:HIS403 4.7 38.3 1.0 CE A:MET235 4.8 50.0 1.0 CG1 A:VAL390 4.9 53.0 1.0 CE2 A:PHE399 4.9 40.1 1.0 CZ A:PHE399 4.9 38.6 1.0

Copper binding site 3 out of 24 in the Crystal Structure of Prophenoloxidase PPO6 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 From Aedes Aegypti within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu701 b:64.5 occ:1.00 NE2 B:HIS210 2.0 70.8 1.0 NE2 B:HIS206 2.0 55.2 1.0 NE2 B:HIS236 2.1 52.1 1.0 CE1 B:HIS206 2.8 54.1 1.0 CE1 B:HIS236 2.9 46.1 1.0 CE1 B:HIS210 2.9 75.0 1.0 CD2 B:HIS210 3.1 70.7 1.0 CD2 B:HIS206 3.1 52.6 1.0 CD2 B:HIS236 3.2 49.6 1.0 CU B:CU702 3.8 56.4 1.0 ND1 B:HIS206 3.9 51.4 1.0 ND1 B:HIS210 4.1 72.9 1.0 ND1 B:HIS236 4.1 43.3 1.0 CG B:HIS206 4.1 51.9 1.0 CG B:HIS210 4.2 70.0 1.0 CG B:HIS236 4.3 46.1 1.0 NE2 B:HIS403 4.5 42.8 1.0 NE2 B:HIS363 4.7 50.5 1.0 CE1 B:HIS363 4.7 51.0 1.0 CE1 B:HIS403 4.8 41.4 1.0 CE B:MET235 4.8 70.0 1.0 CG1 B:VAL390 4.9 53.4 1.0 CE2 B:PHE399 4.9 26.4 1.0 CZ B:PHE399 5.0 26.4 1.0

Copper binding site 4 out of 24 in the Crystal Structure of Prophenoloxidase PPO6 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 From Aedes Aegypti within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu702 b:56.4 occ:1.00 NE2 B:HIS403 2.0 42.8 1.0 NE2 B:HIS363 2.1 50.5 1.0 NE2 B:HIS367 2.1 43.4 1.0 CE1 B:HIS403 2.8 41.4 1.0 CE1 B:HIS367 2.9 40.0 1.0 CE1 B:HIS363 3.0 51.0 1.0 CD2 B:HIS367 3.1 40.6 1.0 CD2 B:HIS363 3.1 46.2 1.0 CD2 B:HIS403 3.1 41.7 1.0 CU B:CU701 3.8 64.5 1.0 CE2 B:PHE399 3.9 26.4 1.0 ND1 B:HIS403 4.0 42.2 1.0 ND1 B:HIS367 4.0 38.3 1.0 CG B:HIS367 4.1 39.4 1.0 ND1 B:HIS363 4.1 49.6 1.0 CG B:HIS403 4.2 41.9 1.0 CG B:HIS363 4.2 46.0 1.0 NE2 B:HIS236 4.3 52.1 1.0 CZ B:PHE399 4.5 26.4 1.0 CZ B:PHE82 4.5 60.6 1.0 CD2 B:HIS236 4.5 49.6 1.0 CD2 B:PHE399 4.6 25.7 1.0 CE1 B:HIS206 4.8 54.1 1.0 NE2 B:HIS206 4.9 55.2 1.0

Copper binding site 5 out of 24 in the Crystal Structure of Prophenoloxidase PPO6 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 From Aedes Aegypti within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu701 b:59.4 occ:1.00 NE2 C:HIS206 2.0 52.8 1.0 NE2 C:HIS210 2.1 60.4 1.0 NE2 C:HIS236 2.1 49.7 1.0 CE1 C:HIS206 2.8 51.6 1.0 CE1 C:HIS236 2.9 48.7 1.0 CE1 C:HIS210 3.0 59.5 1.0 CD2 C:HIS210 3.1 58.4 1.0 CD2 C:HIS206 3.2 46.6 1.0 CD2 C:HIS236 3.2 47.0 1.0 CU C:CU702 3.5 46.9 1.0 ND1 C:HIS206 3.9 47.6 1.0 ND1 C:HIS236 4.1 49.4 1.0 ND1 C:HIS210 4.1 53.4 1.0 CG C:HIS206 4.1 44.2 1.0 CG C:HIS210 4.2 54.5 1.0 CG C:HIS236 4.3 47.9 1.0 NE2 C:HIS403 4.4 41.6 1.0 NE2 C:HIS363 4.5 41.2 1.0 CE1 C:HIS403 4.7 39.4 1.0 CE1 C:HIS363 4.7 42.5 1.0 CE C:MET235 4.9 50.0 1.0 CE2 C:PHE399 4.9 34.6 1.0 CG1 C:VAL390 4.9 44.3 1.0 CZ C:PHE399 4.9 33.3 1.0

Copper binding site 6 out of 24 in the Crystal Structure of Prophenoloxidase PPO6 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 From Aedes Aegypti within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu702 b:46.9 occ:1.00 NE2 C:HIS363 2.1 41.2 1.0 NE2 C:HIS367 2.1 42.9 1.0 NE2 C:HIS403 2.1 41.6 1.0 CE1 C:HIS367 2.9 41.8 1.0 CE1 C:HIS403 2.9 39.4 1.0 CE1 C:HIS363 3.0 42.5 1.0 CD2 C:HIS367 3.1 39.1 1.0 CD2 C:HIS363 3.2 38.4 1.0 CD2 C:HIS403 3.3 38.7 1.0 CU C:CU701 3.5 59.4 1.0 CE2 C:PHE399 3.9 34.6 1.0 ND1 C:HIS367 4.0 40.8 1.0 CG C:HIS367 4.1 39.0 1.0 ND1 C:HIS363 4.1 41.9 1.0 ND1 C:HIS403 4.1 37.3 1.0 NE2 C:HIS236 4.2 49.7 1.0 CG C:HIS363 4.3 36.8 1.0 CG C:HIS403 4.3 37.7 1.0 CZ C:PHE82 4.4 44.2 1.0 CZ C:PHE399 4.5 33.3 1.0 CD2 C:HIS236 4.5 47.0 1.0 CE1 C:HIS206 4.7 51.6 1.0 CD2 C:PHE399 4.7 33.3 1.0 NE2 C:HIS206 4.7 52.8 1.0 CE1 C:PHE82 5.0 47.2 1.0

Copper binding site 7 out of 24 in the Crystal Structure of Prophenoloxidase PPO6 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 From Aedes Aegypti within 5.0Å range: probe atom residue distance (Å) B Occ D:Cu701 b:45.0 occ:1.00 NE2 D:HIS206 2.0 46.4 1.0 NE2 D:HIS210 2.1 44.9 1.0 NE2 D:HIS236 2.1 42.4 1.0 CE1 D:HIS206 2.7 49.1 1.0 CE1 D:HIS236 2.9 42.4 1.0 CE1 D:HIS210 3.0 45.1 1.0 CD2 D:HIS210 3.1 44.0 1.0 CD2 D:HIS206 3.1 46.2 1.0 CD2 D:HIS236 3.2 40.2 1.0 CU D:CU702 3.7 65.5 1.0 ND1 D:HIS206 3.9 50.3 1.0 ND1 D:HIS210 4.1 46.1 1.0 ND1 D:HIS236 4.1 41.4 1.0 CG D:HIS206 4.1 47.8 1.0 CG D:HIS210 4.2 44.7 1.0 CG D:HIS236 4.3 40.3 1.0 NE2 D:HIS403 4.5 47.0 1.0 NE2 D:HIS363 4.7 46.9 1.0 CE1 D:HIS403 4.7 43.3 1.0 CE1 D:HIS363 4.8 46.0 1.0 CE D:MET235 4.8 45.3 1.0 CG1 D:VAL390 4.8 48.9 1.0 CE2 D:PHE399 4.9 30.1 1.0 CZ D:PHE399 4.9 29.7 1.0

Copper binding site 8 out of 24 in the Crystal Structure of Prophenoloxidase PPO6 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 From Aedes Aegypti within 5.0Å range: probe atom residue distance (Å) B Occ D:Cu702 b:65.5 occ:1.00 NE2 D:HIS363 2.0 46.9 1.0 NE2 D:HIS367 2.1 40.2 1.0 NE2 D:HIS403 2.1 47.0 1.0 CE1 D:HIS403 2.9 43.3 1.0 CE1 D:HIS367 2.9 36.2 1.0 CE1 D:HIS363 2.9 46.0 1.0 CD2 D:HIS367 3.0 36.2 1.0 CD2 D:HIS363 3.1 42.8 1.0 CD2 D:HIS403 3.2 43.0 1.0 CU D:CU701 3.7 45.0 1.0 CE2 D:PHE399 4.0 30.1 1.0 ND1 D:HIS367 4.0 35.6 1.0 CG D:HIS367 4.1 35.5 1.0 ND1 D:HIS403 4.1 42.5 1.0 ND1 D:HIS363 4.1 43.5 1.0 CG D:HIS363 4.2 41.6 1.0 CG D:HIS403 4.3 41.2 1.0 NE2 D:HIS236 4.3 42.4 1.0 CZ D:PHE82 4.4 58.6 1.0 CZ D:PHE399 4.6 29.7 1.0 CD2 D:HIS236 4.6 40.2 1.0 CD2 D:PHE399 4.7 29.5 1.0 CE1 D:HIS206 4.8 49.1 1.0 NE2 D:HIS206 4.9 46.4 1.0 CE1 D:PHE82 5.0 62.1 1.0

Copper binding site 9 out of 24 in the Crystal Structure of Prophenoloxidase PPO6 From Aedes Aegypti


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 9 of Crystal Structure of Prophenoloxidase PPO6 From Aedes Aegypti within 5.0Å range: probe atom residue distance (Å) B Occ E:Cu701 b:81.1 occ:1.00 NE2 E:HIS206 2.0 56.1 1.0 NE2 E:HIS210 2.0 68.7 1.0 NE2 E:HIS236 2.1 57.7 1.0 CE1 E:HIS206 2.7 55.5 1.0 CE1 E:HIS236 2.9 50.5 1.0 CE1 E:HIS210 3.0 64.4 1.0 CD2 E:HIS210 3.0 64.1 1.0 CD2 E:HIS206 3.1 53.6 1.0 CD2 E:HIS236 3.2 49.0 1.0 CU E:CU702 3.8 56.8 1.0 ND1 E:HIS206 3.8 56.1 1.0 CG E:HIS206 4.0 55.5 1.0 ND1 E:HIS210 4.1 60.4 1.0 ND1 E:HIS236 4.1 46.2 1.0 CG E:HIS210 4.1 60.3 1.0 CG E:HIS236 4.3 42.6 1.0 NE2 E:HIS403 4.6 40.9 1.0 NE2 E:HIS363 4.7 42.2 1.0 CE1 E:HIS363 4.7 39.6 1.0 CE E:MET235 4.8 47.6 1.0 CE1 E:HIS403 4.8 39.2 1.0 CG1 E:VAL390 4.8 67.6 1.0 CE2 E:PHE399 4.9 28.0 1.0 CZ E:PHE399 4.9 28.2 1.0

Copper binding site 10 out of 24 in the Crystal Structure of Prophenoloxidase PPO6 From Aedes Aegypti


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 10 of Crystal Structure of Prophenoloxidase PPO6 From Aedes Aegypti within 5.0Å range: probe atom residue distance (Å) B Occ E:Cu702 b:56.8 occ:1.00 NE2 E:HIS403 2.0 40.9 1.0 NE2 E:HIS367 2.0 40.1 1.0 NE2 E:HIS363 2.1 42.2 1.0 CE1 E:HIS403 2.8 39.2 1.0 CE1 E:HIS367 2.9 36.9 1.0 CE1 E:HIS363 3.0 39.6 1.0 CD2 E:HIS367 3.0 37.9 1.0 CD2 E:HIS363 3.1 40.5 1.0 CD2 E:HIS403 3.2 36.5 1.0 CU E:CU701 3.8 81.1 1.0 CE2 E:PHE399 3.9 28.0 1.0 ND1 E:HIS367 4.0 35.7 1.0 ND1 E:HIS403 4.0 39.5 1.0 CG E:HIS367 4.1 37.3 1.0 ND1 E:HIS363 4.1 40.4 1.0 CG E:HIS363 4.2 40.9 1.0 CG E:HIS403 4.2 36.2 1.0 NE2 E:HIS236 4.3 57.7 1.0 CZ E:PHE82 4.5 59.7 1.0 CZ E:PHE399 4.5 28.2 1.0 CD2 E:HIS236 4.6 49.0 1.0 CD2 E:PHE399 4.7 28.8 1.0 CE1 E:HIS206 4.8 55.5 1.0 NE2 E:HIS206 4.9 56.1 1.0

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.