Copper in PDB 9fdl: Crystal Structure of the Catalytic Domain of An AA9 Lytic Polysaccharide Monooxygenase From Thermothelomyces Thermophilus (TTLPMO9F)

The structure of Crystal Structure of the Catalytic Domain of An AA9 Lytic Polysaccharide Monooxygenase From Thermothelomyces Thermophilus (TTLPMO9F), PDB code: 9fdl was solved by C.Kosinas, M.Dimarogona, E.Topakas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	131.54 / 2.33
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	55.891, 112.293, 262.381, 90, 90, 90
R / Rfree (%)	16.2 / 20.4

The binding sites of Copper atom in the Crystal Structure of the Catalytic Domain of An AA9 Lytic Polysaccharide Monooxygenase From Thermothelomyces Thermophilus (TTLPMO9F) (pdb code 9fdl). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of the Catalytic Domain of An AA9 Lytic Polysaccharide Monooxygenase From Thermothelomyces Thermophilus (TTLPMO9F), PDB code: 9fdl:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Crystal Structure of the Catalytic Domain of An AA9 Lytic Polysaccharide Monooxygenase From Thermothelomyces Thermophilus (TTLPMO9F)


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 the Catalytic Domain of An AA9 Lytic Polysaccharide Monooxygenase From Thermothelomyces Thermophilus (TTLPMO9F) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu305 b:37.8 occ:0.50 ND1 A:HIS1 2.0 53.2 1.0 NE2 A:HIS84 2.1 42.8 1.0 N A:HIS1 2.1 49.1 1.0 OH A:TYR167 2.6 38.1 1.0 CE1 A:HIS1 2.8 56.8 1.0 CD2 A:HIS84 2.9 38.2 1.0 CG A:HIS1 3.1 57.0 1.0 CE1 A:HIS84 3.2 40.9 1.0 CA A:HIS1 3.3 43.5 1.0 CB A:HIS1 3.6 43.9 1.0 OE1 A:GLN165 3.6 47.9 1.0 CZ A:TYR167 3.7 33.4 1.0 NE2 A:HIS1 4.0 63.6 1.0 CG A:HIS84 4.1 33.8 1.0 CD2 A:HIS1 4.2 56.2 1.0 ND1 A:HIS84 4.2 35.7 1.0 CE2 A:TYR167 4.4 36.3 1.0 CE1 A:TYR167 4.6 32.3 1.0 C A:HIS1 4.6 42.8 1.0 CD A:GLN165 4.7 46.6 1.0

Copper binding site 2 out of 3 in the Crystal Structure of the Catalytic Domain of An AA9 Lytic Polysaccharide Monooxygenase From Thermothelomyces Thermophilus (TTLPMO9F)


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 the Catalytic Domain of An AA9 Lytic Polysaccharide Monooxygenase From Thermothelomyces Thermophilus (TTLPMO9F) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:41.8 occ:0.45 ND1 B:HIS1 2.0 59.1 1.0 N B:HIS1 2.0 53.0 1.0 NE2 B:HIS84 2.1 53.7 1.0 OH B:TYR167 2.7 42.6 1.0 CD2 B:HIS84 2.8 47.1 1.0 CE1 B:HIS1 2.9 65.5 1.0 CG B:HIS1 3.1 60.8 1.0 CA B:HIS1 3.2 57.0 1.0 CE1 B:HIS84 3.2 45.3 1.0 CB B:HIS1 3.6 57.2 1.0 OE1 B:GLN165 3.7 46.7 1.0 CZ B:TYR167 3.8 44.3 1.0 CG B:HIS84 4.0 44.3 1.0 NE2 B:HIS1 4.0 73.9 1.0 CD2 B:HIS1 4.1 69.8 1.0 ND1 B:HIS84 4.1 46.1 1.0 O B:HOH423 4.4 47.9 1.0 CE2 B:TYR167 4.5 48.3 1.0 C B:HIS1 4.5 55.2 1.0 CE1 B:TYR167 4.6 42.1 1.0 CD B:GLN165 4.8 51.0 1.0 O B:HIS1 5.0 55.6 1.0

Copper binding site 3 out of 3 in the Crystal Structure of the Catalytic Domain of An AA9 Lytic Polysaccharide Monooxygenase From Thermothelomyces Thermophilus (TTLPMO9F)


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 the Catalytic Domain of An AA9 Lytic Polysaccharide Monooxygenase From Thermothelomyces Thermophilus (TTLPMO9F) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu301 b:48.6 occ:0.50 ND1 C:HIS1 2.0 67.9 1.0 NE2 C:HIS84 2.1 55.7 1.0 N C:HIS1 2.1 59.5 1.0 OH C:TYR167 2.8 49.6 1.0 CE1 C:HIS1 2.8 75.3 1.0 CD2 C:HIS84 2.9 50.0 1.0 CG C:HIS1 3.1 64.9 1.0 CE1 C:HIS84 3.1 54.2 1.0 O C:HOH477 3.2 42.6 0.5 CA C:HIS1 3.2 57.4 1.0 O C:HOH483 3.3 64.0 1.0 CB C:HIS1 3.5 61.4 1.0 O C:HOH473 3.6 60.4 1.0 OE1 C:GLN165 3.6 50.2 1.0 CZ C:TYR167 3.9 50.6 1.0 NE2 C:HIS1 4.0 79.9 1.0 CD2 C:HIS1 4.1 77.8 1.0 CG C:HIS84 4.1 53.2 1.0 ND1 C:HIS84 4.2 52.6 1.0 C C:HIS1 4.6 53.9 1.0 CE2 C:TYR167 4.6 48.9 1.0 CD C:GLN165 4.7 58.9 1.0 CE1 C:TYR167 4.7 47.0 1.0 O C:HOH410 4.8 53.5 1.0 O C:HOH426 5.0 59.3 1.0

C.Kosinas, K.Chorozian, M.Sandgren, E.Topakas, M.Dimarogona. Mutational Study of A Lytic Polysaccharide Monooxygenase From Myceliophthora Thermophila (MTLPMO9F): Structural Insights Into Substrate Specificity and Regioselectivity. Int.J.Biol.Macromol. V. 288 38574 2024.
ISSN: ISSN 0141-8130
PubMed: 39662565
DOI: 10.1016/J.IJBIOMAC.2024.138574