Copper in PDB 5tkg: Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State

The structure of Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State, PDB code: 5tkg 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)	31.95 / 1.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	67.350, 42.210, 69.480, 90.00, 98.96, 90.00
R / Rfree (%)	11.3 / 14

The binding sites of Copper atom in the Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State (pdb code 5tkg). 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 Resting State, PDB code: 5tkg:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State


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 Resting State within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu303 b:8.4 occ:1.00 ND1 A:HIS1 2.0 8.6 1.0 NE2 A:HIS84 2.0 8.9 1.0 O B:HOH557 2.0 13.7 1.0 N A:HIS1 2.1 8.5 1.0 H3 A:HIS1 2.1 10.2 1.0 O A:HOH647 2.4 17.3 1.0 OH A:TYR168 2.6 7.9 1.0 HH A:TYR168 2.7 9.5 1.0 H2 A:HIS1 2.7 10.2 1.0 CG A:HIS1 3.0 7.5 1.0 CE1 A:HIS1 3.0 8.7 1.0 CE1 A:HIS84 3.0 8.4 1.0 CD2 A:HIS84 3.0 9.0 1.0 CA A:HIS1 3.1 7.0 1.0 HE1 A:HIS84 3.2 10.1 1.0 HE1 A:HIS1 3.2 10.5 1.0 HD2 A:HIS84 3.2 10.8 1.0 HB2 A:HIS1 3.2 8.4 1.0 CB A:HIS1 3.3 7.0 1.0 HA A:HIS1 3.4 8.4 1.0 OE1 A:GLN166 3.7 10.9 1.0 CZ A:TYR168 3.7 7.4 1.0 NE2 A:HIS1 4.1 7.8 1.0 CD2 A:HIS1 4.1 7.4 1.0 ND1 A:HIS84 4.1 9.2 1.0 CG A:HIS84 4.1 9.2 1.0 OE1 B:GLU30 4.2 17.2 0.7 HE1 A:TYR168 4.2 8.4 1.0 O A:HOH528 4.2 10.9 1.0 HB3 A:HIS1 4.2 8.4 1.0 HD3 A:PRO28 4.3 8.6 1.0 O B:HOH821 4.3 29.2 1.0 O B:HOH502 4.4 23.9 1.0 CE1 A:TYR168 4.4 7.0 1.0 HE1 A:HIS157 4.4 13.7 1.0 C A:HIS1 4.4 7.2 1.0 O A:HOH767 4.4 27.7 1.0 CE2 A:TYR168 4.6 7.2 1.0 HE2 A:TYR168 4.6 8.6 1.0 O2 A:OXY401 4.6 19.7 0.5 CD A:GLN166 4.8 10.7 1.0 HG3 A:MET80 4.8 11.3 1.0 HE2 A:HIS1 4.8 9.4 1.0 HD1 A:HIS84 4.9 11.0 1.0 O A:HIS1 4.9 7.5 1.0 HE22 A:GLN166 4.9 15.3 1.0 HD2 A:HIS1 4.9 8.9 1.0 HE2 A:HIS157 5.0 15.3 1.0 HG3 A:PRO28 5.0 9.7 1.0

Copper binding site 2 out of 2 in the Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State


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 Resting State within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu405 b:7.4 occ:1.00 ND1 B:HIS1 2.0 7.9 1.0 O A:HOH432 2.0 12.2 1.0 NE2 B:HIS84 2.0 7.8 1.0 N B:HIS1 2.1 7.2 1.0 H3 B:HIS1 2.3 8.6 1.0 O B:HOH728 2.4 16.1 1.0 OH B:TYR168 2.6 6.5 1.0 H2 B:HIS1 2.7 8.6 1.0 HH B:TYR168 2.7 7.8 1.0 CE1 B:HIS84 2.9 7.8 1.0 CG B:HIS1 3.0 7.1 1.0 CE1 B:HIS1 3.0 7.9 1.0 CD2 B:HIS84 3.0 7.2 1.0 CA B:HIS1 3.1 6.8 1.0 HE1 B:HIS84 3.1 9.4 1.0 HE1 B:HIS1 3.2 9.5 1.0 HD2 B:HIS84 3.2 8.7 1.0 HB2 B:HIS1 3.3 7.8 1.0 CB B:HIS1 3.3 6.5 1.0 HA B:HIS1 3.3 8.1 1.0 CZ B:TYR168 3.6 5.6 1.0 OE1 B:GLN166 3.7 9.7 1.0 OE2 A:GLU30 3.9 15.1 0.6 HE1 B:TYR168 4.0 6.5 1.0 NE2 B:HIS1 4.1 8.2 1.0 ND1 B:HIS84 4.1 7.5 1.0 CD2 B:HIS1 4.1 7.6 1.0 HD3 B:PRO28 4.1 8.6 1.0 CG B:HIS84 4.1 7.1 1.0 O B:HOH578 4.2 9.9 1.0 OE1 A:GLU30 4.2 13.4 0.6 CE1 B:TYR168 4.2 5.4 1.0 HB3 B:HIS1 4.3 7.8 1.0 OE2 A:GLU30 4.3 16.9 0.4 O A:HOH403 4.3 25.5 1.0 C B:HIS1 4.4 6.2 1.0 CD A:GLU30 4.5 13.9 0.6 CE2 B:TYR168 4.6 5.5 1.0 HE1 B:HIS157 4.6 10.9 1.0 HE2 B:TYR168 4.6 6.7 1.0 CD B:GLN166 4.8 9.5 1.0 O B:HOH520 4.8 30.7 1.0 HG3 B:PRO28 4.8 9.1 1.0 HD1 B:HIS84 4.8 9.0 1.0 HE2 B:HIS1 4.8 9.8 1.0 HG3 B:MET80 4.9 8.3 1.0 O B:HIS1 4.9 6.9 1.0 HB2 B:ASP81 4.9 11.8 0.4 O2 B:OXY304 4.9 18.9 0.6 HE22 B:GLN166 4.9 14.2 1.0 HD2 B:HIS1 4.9 9.1 1.0 OE1 A:GLU30 5.0 17.6 0.4 CD B:PRO28 5.0 7.1 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