Copper in PDB 5tkh: Neurospora Crassa Polysaccharide Monooxygenase 2 Ascorbate Treated

The structure of Neurospora Crassa Polysaccharide Monooxygenase 2 Ascorbate Treated, PDB code: 5tkh was solved by W.B.O'dell, F.Meilleur, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.82 / 1.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	67.170, 42.240, 69.370, 90.00, 98.65, 90.00
R / Rfree (%)	12.8 / 15.4

The binding sites of Copper atom in the Neurospora Crassa Polysaccharide Monooxygenase 2 Ascorbate Treated (pdb code 5tkh). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Neurospora Crassa Polysaccharide Monooxygenase 2 Ascorbate Treated, PDB code: 5tkh:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Neurospora Crassa Polysaccharide Monooxygenase 2 Ascorbate Treated


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Neurospora Crassa Polysaccharide Monooxygenase 2 Ascorbate Treated within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu303 b:8.4 occ:1.00 O1 A:PER304 1.9 19.0 0.6 ND1 A:HIS1 1.9 9.2 1.0 NE2 A:HIS84 2.0 7.6 1.0 H3 A:HIS1 2.1 9.2 1.0 N A:HIS1 2.2 7.7 1.0 O A:HOH649 2.4 28.1 0.5 OH A:TYR168 2.7 6.9 1.0 HH A:TYR168 2.7 8.3 1.0 H2 A:HIS1 2.9 9.2 1.0 CG A:HIS1 2.9 7.5 1.0 CE1 A:HIS84 3.0 8.3 1.0 CE1 A:HIS1 3.0 8.8 1.0 CD2 A:HIS84 3.0 6.7 1.0 CA A:HIS1 3.1 6.3 1.0 O2 A:PER304 3.2 19.0 0.6 HE1 A:HIS84 3.2 10.0 1.0 HD2 A:HIS84 3.2 8.0 1.0 HB2 A:HIS1 3.2 8.3 1.0 HE1 A:HIS1 3.2 10.5 1.0 CB A:HIS1 3.2 6.9 1.0 HA A:HIS1 3.4 7.6 1.0 O A:HOH649 3.5 28.0 0.5 OE1 A:GLN166 3.6 9.8 1.0 CZ A:TYR168 3.7 5.5 1.0 NE2 A:HIS1 4.0 8.6 1.0 CD2 A:HIS1 4.0 7.9 1.0 ND1 A:HIS84 4.1 8.1 1.0 CG A:HIS84 4.1 6.8 1.0 HE1 A:TYR168 4.2 6.5 1.0 HB3 A:HIS1 4.2 8.3 1.0 O A:HOH473 4.2 12.4 1.0 HD3 A:PRO28 4.2 7.8 1.0 CE1 A:TYR168 4.4 5.4 1.0 O A:HOH410 4.5 23.0 1.0 OE2 B:GLU30 4.5 19.6 0.5 HE1 A:HIS157 4.5 10.1 1.0 C A:HIS1 4.5 5.8 1.0 CE2 A:TYR168 4.6 5.7 1.0 HE2 A:TYR168 4.6 6.8 1.0 OE1 B:GLU30 4.6 19.2 0.5 CD A:GLN166 4.7 9.8 1.0 HG3 A:MET80 4.8 8.2 1.0 HE2 A:HIS1 4.8 10.3 1.0 HD1 A:HIS84 4.8 9.8 1.0 HB2 A:ASP81 4.9 15.3 0.3 HE22 A:GLN166 4.9 15.3 1.0 HD2 A:HIS1 4.9 9.5 1.0 HG3 A:PRO28 4.9 9.3 1.0 O A:HIS1 4.9 6.7 1.0 HE2 A:HIS157 5.0 13.0 1.0 O A:HOH698 5.0 26.9 1.0

Copper binding site 2 out of 2 in the Neurospora Crassa Polysaccharide Monooxygenase 2 Ascorbate Treated


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Neurospora Crassa Polysaccharide Monooxygenase 2 Ascorbate Treated within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu303 b:9.1 occ:1.00 H3 B:HIS1 1.9 9.7 1.0 ND1 B:HIS1 1.9 9.2 1.0 NE2 B:HIS84 2.0 9.5 1.0 O B:HOH405 2.1 34.6 0.6 N B:HIS1 2.2 8.1 1.0 O B:HOH677 2.2 29.2 0.3 HH B:TYR168 2.7 9.4 1.0 OH B:TYR168 2.7 7.8 1.0 H2 B:HIS1 2.9 9.7 1.0 CG B:HIS1 2.9 7.5 1.0 CD2 B:HIS84 2.9 9.3 1.0 CE1 B:HIS1 3.0 9.1 1.0 CE1 B:HIS84 3.0 9.4 1.0 HD2 B:HIS84 3.1 11.1 1.0 HB2 B:HIS1 3.1 8.8 1.0 CA B:HIS1 3.1 7.2 1.0 HE1 B:HIS1 3.2 10.9 1.0 HE1 B:HIS84 3.2 11.3 1.0 CB B:HIS1 3.2 7.3 1.0 O B:HOH677 3.4 28.4 0.7 HA B:HIS1 3.4 8.6 1.0 O1 B:OXY305 3.6 26.3 0.6 OE1 B:GLN166 3.6 12.4 1.0 CZ B:TYR168 3.8 6.7 1.0 O B:HOH750 4.0 22.8 1.0 NE2 B:HIS1 4.1 8.2 1.0 CD2 B:HIS1 4.1 8.3 1.0 ND1 B:HIS84 4.1 9.8 1.0 CG B:HIS84 4.1 9.1 1.0 HB3 B:HIS1 4.2 8.8 1.0 O B:HOH503 4.3 11.9 1.0 HE1 B:TYR168 4.3 8.1 1.0 HE1 B:HIS157 4.3 12.3 1.0 HD3 B:PRO28 4.3 9.3 1.0 O A:HOH423 4.4 24.4 1.0 CE1 B:TYR168 4.5 6.7 1.0 OE1 A:GLU30 4.5 17.7 0.6 C B:HIS1 4.5 6.7 1.0 HE2 B:TYR168 4.6 8.3 1.0 CE2 B:TYR168 4.6 6.9 1.0 CD B:GLN166 4.7 12.3 1.0 HG3 B:MET80 4.8 10.8 1.0 HE22 B:GLN166 4.8 17.5 1.0 O2 B:OXY305 4.8 26.1 0.6 HE2 B:HIS1 4.8 9.9 1.0 HE2 B:HIS157 4.8 14.8 1.0 HD1 B:HIS84 4.9 11.7 1.0 O B:HIS1 4.9 7.3 1.0 HD2 B:HIS1 4.9 10.0 1.0

W.B.O'dell, P.K.Agarwal, F.Meilleur. Oxygen Activation at the Active Site of A Fungal Lytic Polysaccharide Monooxygenase. Angew. Chem. Int. Ed. Engl. V. 56 767 2017.
ISSN: ESSN 1521-3773
PubMed: 28004877
DOI: 10.1002/ANIE.201610502