Copper in PDB 5tki: Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State Joint X-Ray/Neutron Refinement

The structure of Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State Joint X-Ray/Neutron Refinement, PDB code: 5tki 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)	N/A / 1.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	68.120, 42.230, 70.290, 90.00, 98.33, 90.00
R / Rfree (%)	21.6 / 25.3

The binding sites of Copper atom in the Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State Joint X-Ray/Neutron Refinement (pdb code 5tki). 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 Joint X-Ray/Neutron Refinement, PDB code: 5tki:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State Joint X-Ray/Neutron Refinement


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 Joint X-Ray/Neutron Refinement within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu303 b:14.9 occ:1.00 NE2 A:HIS84 2.0 10.2 1.0 ND1 A:HIS1 2.0 11.1 1.0 O B:HOH411 2.0 15.1 1.0 N A:HIS1 2.1 11.3 1.0 D2 A:HIS1 2.4 13.6 1.0 D1 B:HOH411 2.4 18.1 1.0 O A:HOH558 2.4 18.5 1.0 D3 A:HIS1 2.5 13.6 1.0 D2 B:HOH411 2.6 18.1 1.0 D2 A:HOH558 2.7 22.2 1.0 OH A:TYR168 2.7 13.9 1.0 CE1 A:HIS84 2.9 13.2 1.0 DH A:TYR168 2.9 16.7 1.0 CE1 A:HIS1 3.0 12.8 1.0 HE1 A:HIS84 3.0 15.9 1.0 CG A:HIS1 3.0 14.0 1.0 CD2 A:HIS84 3.1 11.5 1.0 CA A:HIS1 3.1 9.8 1.0 D1 A:HOH558 3.1 22.2 1.0 HE1 A:HIS1 3.2 15.4 1.0 HD2 A:HIS84 3.3 13.8 1.0 HA A:HIS1 3.3 11.8 1.0 CB A:HIS1 3.4 12.7 1.0 HB2 A:HIS1 3.4 15.3 1.0 D2 A:HOH486 3.6 22.1 1.0 CZ A:TYR168 3.7 11.7 1.0 OE1 A:GLN166 3.7 13.7 1.0 ND1 A:HIS84 4.0 14.6 1.0 NE2 A:HIS1 4.1 16.2 1.0 OE1 B:GLU30 4.1 23.9 1.0 HE1 A:TYR168 4.1 12.7 1.0 CD2 A:HIS1 4.1 14.2 1.0 CG A:HIS84 4.1 14.9 1.0 D1 B:HOH447 4.2 35.8 1.0 O B:HOH447 4.2 29.8 1.0 O A:HOH486 4.2 18.4 1.0 D1 A:HOH486 4.2 22.1 1.0 HB3 A:HIS1 4.3 15.3 1.0 CE1 A:TYR168 4.3 10.6 1.0 HD3 A:PRO28 4.3 16.4 1.0 D2 B:HOH447 4.4 35.8 1.0 C A:HIS1 4.4 10.8 1.0 CE2 A:TYR168 4.6 10.9 1.0 HE2 A:TYR168 4.7 13.1 1.0 HE1 A:HIS157 4.7 16.2 1.0 HG3 A:MET80 4.8 15.8 1.0 DD1 A:HIS84 4.8 17.5 1.0 CD A:GLN166 4.8 14.6 1.0 D1 A:HOH571 4.8 35.8 1.0 DE2 A:HIS1 4.8 19.4 1.0 O A:HIS1 4.9 13.1 1.0 HG3 A:PRO28 4.9 17.6 1.0 HD2 A:HIS1 5.0 17.1 1.0 O A:HOH571 5.0 29.9 1.0 D2 A:HOH506 5.0 32.4 1.0

Copper binding site 2 out of 2 in the Neurospora Crassa Polysaccharide Monooxygenase 2 Resting State Joint X-Ray/Neutron Refinement


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 Joint X-Ray/Neutron Refinement within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu303 b:17.0 occ:1.00 O A:HOH419 1.9 14.1 1.0 ND1 B:HIS1 2.0 16.1 1.0 NE2 B:HIS84 2.0 18.0 1.0 N B:HIS1 2.0 10.3 1.0 D2 A:HOH419 2.4 17.0 1.0 DH B:TYR168 2.4 18.0 1.0 D3 B:HIS1 2.4 12.4 1.0 O B:HOH534 2.5 18.4 1.0 D1 A:HOH419 2.5 17.0 1.0 D2 B:HIS1 2.6 12.4 1.0 OH B:TYR168 2.7 15.0 1.0 D2 B:HOH534 2.8 22.1 1.0 D1 B:HOH534 2.9 22.1 1.0 CE1 B:HIS84 2.9 16.4 1.0 CG B:HIS1 3.0 11.4 1.0 CE1 B:HIS1 3.0 16.5 1.0 HE1 B:HIS84 3.0 19.7 1.0 CD2 B:HIS84 3.1 12.6 1.0 CA B:HIS1 3.1 11.5 1.0 HE1 B:HIS1 3.2 19.8 1.0 HD2 B:HIS84 3.3 15.1 1.0 CB B:HIS1 3.3 14.3 1.0 HA B:HIS1 3.4 13.8 1.0 HB2 B:HIS1 3.4 17.2 1.0 D1 A:HOH406 3.7 42.4 1.0 D2 B:HOH449 3.7 25.4 1.0 OE1 B:GLN166 3.7 16.4 1.0 CZ B:TYR168 3.7 14.7 1.0 ND1 B:HIS84 4.1 17.0 1.0 NE2 B:HIS1 4.1 15.1 1.0 CD2 B:HIS1 4.1 15.0 1.0 OE2 A:GLU30 4.1 34.4 0.6 OE1 A:GLU30 4.2 33.3 0.4 D2 A:HOH406 4.2 42.4 1.0 CG B:HIS84 4.2 14.9 1.0 O B:HOH449 4.2 21.1 1.0 HE1 B:TYR168 4.2 15.1 1.0 HB3 B:HIS1 4.3 17.2 1.0 O A:HOH406 4.3 35.3 1.0 HD3 B:PRO28 4.4 18.5 1.0 CE1 B:TYR168 4.4 12.6 1.0 C B:HIS1 4.4 18.0 1.0 HE1 B:HIS157 4.5 23.0 1.0 HE2 B:TYR168 4.6 15.4 1.0 D1 B:HOH449 4.6 25.4 1.0 CE2 B:TYR168 4.6 12.9 1.0 HG3 B:MET80 4.8 23.9 1.0 CD B:GLN166 4.8 15.1 1.0 DD1 B:HIS84 4.8 20.4 1.0 DE2 B:HIS1 4.9 18.1 1.0 O B:HIS1 4.9 14.5 1.0 HD2 B:HIS1 5.0 18.0 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