Copper in PDB 5wsz: Crystal Structure of A Lytic Polysaccharide Monooxygenase,BTLPMO10A, From Bacillus Thuringiensis

The structure of Crystal Structure of A Lytic Polysaccharide Monooxygenase,BTLPMO10A, From Bacillus Thuringiensis, PDB code: 5wsz was solved by Y.Zhao, H.Zhang, H.Yin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.12 / 2.57
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	73.021, 73.446, 113.583, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 25

The binding sites of Copper atom in the Crystal Structure of A Lytic Polysaccharide Monooxygenase,BTLPMO10A, From Bacillus Thuringiensis (pdb code 5wsz). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of A Lytic Polysaccharide Monooxygenase,BTLPMO10A, From Bacillus Thuringiensis, PDB code: 5wsz:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Crystal Structure of A Lytic Polysaccharide Monooxygenase,BTLPMO10A, From Bacillus Thuringiensis


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 A Lytic Polysaccharide Monooxygenase,BTLPMO10A, From Bacillus Thuringiensis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu200 b:31.4 occ:1.00 N A:HIS1 2.0 29.3 1.0 ND1 A:HIS1 2.0 29.3 1.0 NE2 A:HIS85 2.1 38.7 1.0 CD2 A:HIS85 2.9 36.6 1.0 CA A:HIS1 3.0 26.7 1.0 CG A:HIS1 3.0 25.5 1.0 CE1 A:HIS1 3.0 30.2 1.0 CB A:HIS1 3.3 25.4 1.0 CE1 A:HIS85 3.3 39.1 1.0 CZ A:PHE158 3.4 35.8 1.0 CE1 A:PHE158 4.0 30.1 1.0 CB A:ALA83 4.1 33.4 1.0 CD2 A:HIS1 4.1 25.1 1.0 O A:ALA83 4.1 30.5 1.0 NE2 A:HIS1 4.1 27.0 1.0 CG A:HIS85 4.1 35.7 1.0 CE2 A:PHE158 4.2 30.5 1.0 ND1 A:HIS85 4.3 35.4 1.0 C A:HIS1 4.3 25.0 1.0 O D:ALA152 4.4 39.1 1.0 O D:ASP153 4.4 31.3 1.0 O A:HIS1 4.7 28.7 1.0 C A:ALA83 4.9 31.7 1.0

Copper binding site 2 out of 4 in the Crystal Structure of A Lytic Polysaccharide Monooxygenase,BTLPMO10A, From Bacillus Thuringiensis


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 A Lytic Polysaccharide Monooxygenase,BTLPMO10A, From Bacillus Thuringiensis within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu200 b:76.3 occ:1.00 ND1 B:HIS1 2.1 54.5 1.0 N B:HIS1 2.2 58.0 1.0 CE1 B:HIS85 2.8 83.4 1.0 CE1 B:HIS1 2.9 54.8 1.0 CG B:HIS1 3.0 52.1 1.0 CA B:HIS1 3.1 47.4 1.0 ND1 B:HIS85 3.1 78.9 1.0 CZ B:PHE158 3.4 41.3 1.0 CB B:HIS1 3.5 48.0 1.0 NE2 B:HIS85 3.7 78.9 1.0 CE1 B:PHE158 3.9 38.5 1.0 NE2 B:HIS1 3.9 53.5 1.0 CD2 B:HIS1 4.0 51.9 1.0 CG B:HIS85 4.1 76.8 1.0 O B:ALA83 4.1 66.5 1.0 CB B:ALA83 4.1 61.5 1.0 CE2 B:PHE158 4.3 40.3 1.0 CD2 B:HIS85 4.4 76.5 1.0 C B:HIS1 4.4 44.1 1.0 O B:HIS1 4.9 46.0 1.0 C B:ALA83 5.0 64.3 1.0

Copper binding site 3 out of 4 in the Crystal Structure of A Lytic Polysaccharide Monooxygenase,BTLPMO10A, From Bacillus Thuringiensis


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 A Lytic Polysaccharide Monooxygenase,BTLPMO10A, From Bacillus Thuringiensis within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu200 b:52.9 occ:1.00 ND1 C:HIS1 1.9 36.1 1.0 NE2 C:HIS85 2.0 54.2 1.0 N C:HIS1 2.0 40.0 1.0 CD2 C:HIS85 2.7 46.2 1.0 CG C:HIS1 2.9 36.3 1.0 CE1 C:HIS1 3.0 36.3 1.0 CA C:HIS1 3.0 32.8 1.0 CE1 C:HIS85 3.1 53.1 1.0 CB C:HIS1 3.2 37.1 1.0 CZ C:PHE158 3.5 39.4 1.0 CB C:ALA83 3.9 37.8 1.0 O C:ALA83 3.9 47.3 1.0 CG C:HIS85 4.0 43.0 1.0 CD2 C:HIS1 4.0 36.0 1.0 NE2 C:HIS1 4.0 40.9 1.0 CE1 C:PHE158 4.1 34.1 1.0 ND1 C:HIS85 4.1 49.8 1.0 C C:HIS1 4.3 32.2 1.0 CE2 C:PHE158 4.4 33.5 1.0 O C:HIS1 4.7 35.4 1.0 C C:ALA83 4.7 45.3 1.0 CA C:ALA83 4.8 41.8 1.0

Copper binding site 4 out of 4 in the Crystal Structure of A Lytic Polysaccharide Monooxygenase,BTLPMO10A, From Bacillus Thuringiensis


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 A Lytic Polysaccharide Monooxygenase,BTLPMO10A, From Bacillus Thuringiensis within 5.0Å range: probe atom residue distance (Å) B Occ D:Cu200 b:92.2 occ:1.00 ND1 D:HIS1 2.4 46.8 1.0 CB D:ALA83 2.7 65.8 1.0 CA D:HIS1 2.7 54.6 1.0 N D:HIS1 3.2 61.9 1.0 ND1 D:HIS85 3.3 63.9 1.0 CE1 D:HIS85 3.3 66.0 1.0 CG D:HIS1 3.3 49.2 1.0 CE1 D:HIS1 3.5 45.9 1.0 CB D:HIS1 3.5 48.4 1.0 CZ D:PHE158 3.6 35.3 1.0 C D:HIS1 3.8 48.7 1.0 CE1 D:PHE158 4.1 29.8 1.0 O D:HIS1 4.1 53.9 1.0 CA D:ALA83 4.2 63.0 1.0 NE2 D:HIS85 4.2 66.0 1.0 CG D:HIS85 4.3 58.8 1.0 CE2 D:PHE158 4.5 33.7 1.0 CD2 D:HIS1 4.5 46.7 1.0 NE2 D:HIS1 4.5 47.0 1.0 N D:ALA83 4.7 56.4 1.0 CZ3 D:TRP149 4.7 46.0 1.0 CD2 D:HIS85 4.8 61.9 1.0 CH2 D:TRP149 4.8 50.8 1.0 N D:GLY2 4.8 45.6 1.0 C D:ALA83 4.9 66.6 1.0

Y.Zhao, H.Zhang, H.Yin. Crystal Structure of A Lytic Polysaccharide Monooxygenase,BTLPMO10A, From Bacillus Thuringiensis To Be Published.