Copper in PDB 5tkf: Neurospora Crassa Polysaccharide Monooxygenase 2 High Mannosylation

The structure of Neurospora Crassa Polysaccharide Monooxygenase 2 High Mannosylation, PDB code: 5tkf 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)	40.31 / 2.10
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	43.300, 67.040, 84.150, 97.57, 97.61, 97.43
R / Rfree (%)	14.2 / 17.7

The binding sites of Copper atom in the Neurospora Crassa Polysaccharide Monooxygenase 2 High Mannosylation (pdb code 5tkf). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Neurospora Crassa Polysaccharide Monooxygenase 2 High Mannosylation, PDB code: 5tkf:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Neurospora Crassa Polysaccharide Monooxygenase 2 High Mannosylation


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 High Mannosylation within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu308 b:11.2 occ:1.00 ND1 A:HIS1 1.9 11.9 1.0 NE2 A:HIS84 2.0 15.2 1.0 H3 A:HIS1 2.1 9.9 1.0 N A:HIS1 2.2 8.2 1.0 OH A:TYR168 2.7 10.0 1.0 HH A:TYR168 2.8 12.0 1.0 H2 A:HIS1 2.9 9.9 1.0 CD2 A:HIS84 2.9 12.7 1.0 O B:HOH405 2.9 34.4 1.0 CG A:HIS1 2.9 11.2 1.0 CE1 A:HIS1 2.9 13.4 1.0 HD2 A:HIS84 3.0 15.3 1.0 CE1 A:HIS84 3.0 15.1 1.0 HE1 A:HIS1 3.1 16.1 1.0 CA A:HIS1 3.2 8.3 1.0 HB2 A:HIS1 3.2 11.2 1.0 CB A:HIS1 3.3 9.4 1.0 HE1 A:HIS84 3.3 18.1 1.0 HA A:HIS1 3.5 10.0 1.0 O A:HOH648 3.5 28.0 1.0 OE1 A:GLN166 3.5 12.7 1.0 CZ A:TYR168 3.7 9.4 1.0 NE2 A:HIS1 4.0 14.1 1.0 CD2 A:HIS1 4.0 12.2 1.0 CG A:HIS84 4.0 11.7 1.0 ND1 A:HIS84 4.1 14.7 1.0 HE2 A:TYR168 4.2 10.7 1.0 O A:HOH474 4.2 6.5 1.0 HB3 A:HIS1 4.2 11.2 1.0 HE1 A:HIS157 4.3 20.3 1.0 CE2 A:TYR168 4.4 8.9 1.0 HD3 A:PRO28 4.5 15.5 1.0 C A:HIS1 4.5 8.1 1.0 CE1 A:TYR168 4.6 9.3 1.0 HE1 A:TYR168 4.6 11.2 1.0 HG3 A:MET80 4.6 13.2 1.0 CD A:GLN166 4.6 12.3 1.0 HE22 A:GLN166 4.8 17.2 1.0 HE2 A:HIS1 4.8 16.9 1.0 HE2 A:HIS157 4.8 21.2 1.0 O A:HIS1 4.9 8.1 1.0 HD1 A:HIS84 4.9 17.7 1.0 HG3 A:PRO28 4.9 16.1 1.0 HD2 A:HIS1 4.9 14.6 1.0 CE1 A:HIS157 5.0 16.9 1.0

Copper binding site 2 out of 4 in the Neurospora Crassa Polysaccharide Monooxygenase 2 High Mannosylation


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 High Mannosylation within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu303 b:12.1 occ:1.00 H3 B:HIS1 2.0 10.5 1.0 NE2 B:HIS84 2.0 11.6 1.0 ND1 B:HIS1 2.0 7.9 1.0 N B:HIS1 2.2 8.8 1.0 HH B:TYR168 2.6 11.5 1.0 OH B:TYR168 2.7 9.6 1.0 H2 B:HIS1 2.9 10.5 1.0 CD2 B:HIS84 2.9 12.1 1.0 CG B:HIS1 3.0 8.2 1.0 CE1 B:HIS1 3.0 7.7 1.0 HD2 B:HIS84 3.1 14.5 1.0 CE1 B:HIS84 3.1 12.7 1.0 CA B:HIS1 3.2 8.6 1.0 HB2 B:HIS1 3.2 11.2 1.0 HE1 B:HIS1 3.2 9.3 1.0 O A:HOH418 3.3 43.2 1.0 CB B:HIS1 3.3 9.3 1.0 HE1 B:HIS84 3.3 15.2 1.0 HA B:HIS1 3.5 10.3 1.0 OE1 B:GLN166 3.5 12.8 1.0 O2 B:OXY309 3.5 41.6 0.8 CZ B:TYR168 3.8 9.2 1.0 O B:HOH632 3.9 28.5 1.0 O B:HOH476 4.1 11.0 1.0 CG B:HIS84 4.1 12.1 1.0 ND1 B:HIS84 4.1 12.6 1.0 NE2 B:HIS1 4.1 7.9 1.0 CD2 B:HIS1 4.1 8.0 1.0 HB3 B:HIS1 4.3 11.2 1.0 OE2 A:GLU30 4.3 29.7 1.0 HE1 B:HIS157 4.3 16.4 1.0 HE1 B:TYR168 4.4 10.7 1.0 C B:HIS1 4.5 9.5 1.0 HE2 B:TYR168 4.5 10.9 1.0 HD3 B:PRO28 4.5 12.9 1.0 CE1 B:TYR168 4.5 8.9 1.0 CD B:GLN166 4.5 13.4 1.0 HE22 B:GLN166 4.5 17.2 1.0 CE2 B:TYR168 4.6 9.1 1.0 O1 B:OXY309 4.7 41.4 0.8 HG3 B:PRO28 4.8 13.8 1.0 HE2 B:HIS157 4.8 15.4 1.0 HG3 B:MET80 4.8 14.5 1.0 HE2 B:HIS1 4.9 9.4 1.0 HD1 B:HIS84 4.9 15.1 1.0 O B:HIS1 4.9 10.3 1.0 CE1 B:HIS157 4.9 13.7 1.0 NE2 B:GLN166 4.9 14.3 1.0 HD2 B:HIS1 5.0 9.6 1.0

Copper binding site 3 out of 4 in the Neurospora Crassa Polysaccharide Monooxygenase 2 High Mannosylation


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Neurospora Crassa Polysaccharide Monooxygenase 2 High Mannosylation within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu305 b:16.6 occ:1.00 ND1 C:HIS1 2.0 18.6 1.0 H3 C:HIS1 2.0 14.0 1.0 NE2 C:HIS84 2.0 18.3 1.0 N C:HIS1 2.2 11.7 1.0 OH C:TYR168 2.6 13.4 1.0 HH C:TYR168 2.7 16.1 1.0 H2 C:HIS1 2.9 14.0 1.0 CD2 C:HIS84 2.9 17.4 1.0 CG C:HIS1 3.0 16.0 1.0 CE1 C:HIS1 3.0 18.1 1.0 CE1 C:HIS84 3.0 18.9 1.0 HD2 C:HIS84 3.1 20.9 1.0 CA C:HIS1 3.2 12.3 1.0 HE1 C:HIS1 3.2 21.8 1.0 HB2 C:HIS1 3.2 16.2 1.0 HE1 C:HIS84 3.2 22.7 1.0 CB C:HIS1 3.3 13.6 1.0 HA C:HIS1 3.4 14.8 1.0 OE1 C:GLN166 3.6 16.9 1.0 CZ C:TYR168 3.7 11.9 1.0 O C:HOH616 3.9 27.8 1.0 NE2 C:HIS1 4.1 18.5 1.0 CG C:HIS84 4.1 18.2 1.0 ND1 C:HIS84 4.1 19.4 1.0 CD2 C:HIS1 4.1 17.4 1.0 HE2 C:TYR168 4.2 12.8 1.0 HB3 C:HIS1 4.2 16.2 1.0 HE1 C:HIS157 4.3 25.3 1.0 O C:HOH417 4.3 11.1 1.0 CE2 C:TYR168 4.4 10.7 1.0 HD3 C:PRO28 4.4 15.8 1.0 C C:HIS1 4.5 11.4 1.0 HE1 C:TYR168 4.5 14.8 1.0 CE1 C:TYR168 4.6 12.3 1.0 CD C:GLN166 4.6 17.5 1.0 HE22 C:GLN166 4.6 22.8 1.0 HG3 C:MET80 4.7 21.2 1.0 HE2 C:HIS1 4.8 22.2 1.0 HD1 C:HIS84 4.9 23.3 1.0 HE2 C:HIS157 4.9 26.5 1.0 HG3 C:PRO28 4.9 16.0 1.0 HD2 C:HIS1 4.9 20.9 1.0 O C:HIS1 4.9 12.0 1.0 CE1 C:HIS157 5.0 21.1 1.0

Copper binding site 4 out of 4 in the Neurospora Crassa Polysaccharide Monooxygenase 2 High Mannosylation


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Neurospora Crassa Polysaccharide Monooxygenase 2 High Mannosylation within 5.0Å range: probe atom residue distance (Å) B Occ D:Cu302 b:19.1 occ:1.00 ND1 D:HIS1 2.0 16.5 1.0 NE2 D:HIS84 2.0 20.1 1.0 H3 D:HIS1 2.0 13.7 1.0 N D:HIS1 2.2 11.4 1.0 HH D:TYR168 2.7 13.6 1.0 OH D:TYR168 2.7 11.3 1.0 H2 D:HIS1 2.9 13.7 1.0 CG D:HIS1 2.9 14.7 1.0 CD2 D:HIS84 2.9 18.4 1.0 CE1 D:HIS1 3.0 15.6 1.0 CE1 D:HIS84 3.0 19.4 1.0 O D:HOH544 3.1 45.7 1.0 HD2 D:HIS84 3.1 22.1 1.0 HB2 D:HIS1 3.1 16.4 1.0 CA D:HIS1 3.2 11.5 1.0 HE1 D:HIS1 3.2 18.8 1.0 CB D:HIS1 3.2 13.7 1.0 HE1 D:HIS84 3.3 23.3 1.0 HA D:HIS1 3.4 13.8 1.0 OE1 D:GLN166 3.5 14.8 1.0 O1 D:OXY303 3.6 41.7 0.8 CZ D:TYR168 3.8 10.9 1.0 CD2 D:HIS1 4.1 15.7 1.0 NE2 D:HIS1 4.1 15.8 1.0 CG D:HIS84 4.1 17.9 1.0 ND1 D:HIS84 4.1 19.6 1.0 O D:HOH589 4.1 29.3 1.0 O D:HOH481 4.2 11.8 1.0 HB3 D:HIS1 4.2 16.4 1.0 HE1 D:HIS157 4.3 15.1 1.0 HE1 D:TYR168 4.4 12.9 1.0 HD3 D:PRO28 4.4 14.4 1.0 C D:HIS1 4.5 12.2 1.0 CE1 D:TYR168 4.5 10.8 1.0 HE2 D:TYR168 4.5 13.0 1.0 CD D:GLN166 4.5 14.9 1.0 HE22 D:GLN166 4.6 19.6 1.0 CE2 D:TYR168 4.6 10.9 1.0 HG3 D:MET80 4.7 21.8 1.0 O2 D:OXY303 4.7 41.2 0.8 HE2 D:HIS157 4.7 17.1 1.0 HE2 D:HIS1 4.9 18.9 1.0 HG3 D:PRO28 4.9 15.5 1.0 HD1 D:HIS84 4.9 23.6 1.0 O D:HIS1 4.9 14.0 1.0 CE1 D:HIS157 4.9 12.5 1.0 HD2 D:HIS1 4.9 18.9 1.0 NE2 D:GLN166 5.0 16.4 1.0

W.B.O'dell, P.D.Swartz, K.L.Weiss, F.Meilleur. Crystallization of A Fungal Lytic Polysaccharide Monooxygenase Expressed From Glycoengineered Pichia Pastoris For X-Ray and Neutron Diffraction. Acta Crystallogr F Struct V. 73 70 2017BIOL Commun.
ISSN: ESSN 2053-230X
PubMed: 28177316
DOI: 10.1107/S2053230X16020318