Copper in PDB 7t5e: Neutron Structure of Neurospora Crassa Polysaccharide Monooxygenase 9D (NCLPMO9D) Low pH Vapor Exchange

The structure of Neutron Structure of Neurospora Crassa Polysaccharide Monooxygenase 9D (NCLPMO9D) Low pH Vapor Exchange, PDB code: 7t5e was solved by G.C.Schroder, F.Meilleur, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	68.296, 42.269, 70.413, 90, 98.47, 90
R / Rfree (%)	14.4 / 21.4

The binding sites of Copper atom in the Neutron Structure of Neurospora Crassa Polysaccharide Monooxygenase 9D (NCLPMO9D) Low pH Vapor Exchange (pdb code 7t5e). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Neutron Structure of Neurospora Crassa Polysaccharide Monooxygenase 9D (NCLPMO9D) Low pH Vapor Exchange, PDB code: 7t5e:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Neutron Structure of Neurospora Crassa Polysaccharide Monooxygenase 9D (NCLPMO9D) Low pH Vapor Exchange


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Neutron Structure of Neurospora Crassa Polysaccharide Monooxygenase 9D (NCLPMO9D) Low pH Vapor Exchange within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:19.1 occ:1.00 ND1 A:HIS1 2.0 16.3 1.0 NE2 A:HIS84 2.0 16.8 1.0 O B:HOH411 2.1 19.3 1.0 N A:HIS1 2.1 13.0 1.0 O A:HOH491 2.3 27.6 1.0 D3 A:HIS1 2.5 17.1 1.0 D2 A:HIS1 2.6 14.1 1.0 D2 B:HOH411 2.6 15.3 1.0 OH A:TYR168 2.7 12.9 1.0 D1 B:HOH411 2.8 21.2 1.0 DH A:TYR168 2.9 14.2 1.0 CE1 A:HIS84 2.9 23.1 1.0 D1 A:HOH491 2.9 15.6 1.0 CG A:HIS1 2.9 16.4 1.0 CE1 A:HIS1 3.0 15.4 1.0 D2 A:HOH491 3.0 24.6 1.0 CD2 A:HIS84 3.1 16.1 1.0 CA A:HIS1 3.1 13.8 1.0 HE1 A:HIS84 3.1 16.3 1.0 HB2 A:HIS1 3.2 24.0 1.0 CB A:HIS1 3.2 17.5 1.0 HE1 A:HIS1 3.3 17.4 1.0 HD2 A:HIS84 3.3 16.9 1.0 HA A:HIS1 3.4 15.2 1.0 OE1 A:GLN166 3.7 14.8 1.0 CZ A:TYR168 3.8 15.3 1.0 D2 B:HOH473 3.8 17.5 1.0 ND1 A:HIS84 4.1 19.1 1.0 CD2 A:HIS1 4.1 14.7 1.0 OE2 B:GLU30 4.1 31.5 1.0 NE2 A:HIS1 4.1 20.1 1.0 O A:HOH519 4.1 23.4 1.0 CG A:HIS84 4.2 18.1 1.0 D2 A:HOH519 4.2 21.3 1.0 D1 A:HOH519 4.2 41.7 1.0 HD3 A:PRO28 4.2 14.3 1.0 HE1 A:TYR168 4.3 12.0 1.0 HB3 A:HIS1 4.3 18.8 1.0 O B:HOH473 4.3 39.9 1.0 C A:HIS1 4.4 16.5 1.0 CE1 A:TYR168 4.4 14.7 1.0 HE1 A:HIS157 4.5 18.3 1.0 O A:HOH552 4.6 45.0 1.0 CE2 A:TYR168 4.6 14.6 1.0 HE2 A:TYR168 4.7 13.8 1.0 HG3 A:MET80 4.7 14.1 1.0 D2 A:HOH552 4.8 35.6 1.0 O A:HIS1 4.8 13.2 1.0 CD A:GLN166 4.8 18.1 1.0 D1 B:HOH473 4.8 39.9 1.0 DE21 A:GLN166 4.9 24.4 0.8 D1 A:HOH552 4.9 35.2 1.0 DD1 A:HIS84 5.0 22.1 1.0 HB3 A:ASP81 5.0 23.7 1.0

Copper binding site 2 out of 2 in the Neutron Structure of Neurospora Crassa Polysaccharide Monooxygenase 9D (NCLPMO9D) Low pH Vapor Exchange


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Neutron Structure of Neurospora Crassa Polysaccharide Monooxygenase 9D (NCLPMO9D) Low pH Vapor Exchange within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:16.8 occ:1.00 ND1 B:HIS1 2.0 14.7 1.0 N B:HIS1 2.0 15.3 1.0 O A:HOH410 2.0 15.5 1.0 NE2 B:HIS84 2.0 10.9 1.0 D1 A:HOH410 2.2 20.5 1.0 D2 B:HIS1 2.4 9.1 1.0 O B:HOH545 2.4 20.4 1.0 D3 B:HIS1 2.5 8.0 1.0 OH B:TYR168 2.7 13.2 1.0 D2 B:HOH545 2.9 20.1 1.0 D2 A:HOH410 2.9 16.3 1.0 CG B:HIS1 3.0 11.7 1.0 CE1 B:HIS1 3.0 13.0 1.0 DH B:TYR168 3.0 12.5 0.7 CE1 B:HIS84 3.0 13.5 1.0 CA B:HIS1 3.1 15.6 1.0 CD2 B:HIS84 3.1 14.6 1.0 HE1 B:HIS84 3.2 18.9 1.0 HE1 B:HIS1 3.2 11.9 1.0 D1 B:HOH545 3.3 24.9 1.0 HA B:HIS1 3.3 12.2 1.0 CB B:HIS1 3.3 16.9 1.0 HD2 B:HIS84 3.3 16.5 1.0 HB2 B:HIS1 3.4 16.6 1.0 CZ B:TYR168 3.7 14.2 1.0 OE1 B:GLN166 3.7 14.5 1.0 O B:HOH476 4.1 16.3 1.0 D1 B:HOH476 4.1 20.2 1.0 NE2 B:HIS1 4.1 12.2 1.0 CD2 B:HIS1 4.1 14.3 1.0 OE1 A:GLU30 4.1 24.5 1.0 ND1 B:HIS84 4.1 14.5 1.0 HD3 B:PRO28 4.1 18.0 1.0 HE1 B:TYR168 4.2 14.9 1.0 CG B:HIS84 4.2 15.3 1.0 O A:HOH507 4.2 33.7 1.0 D2 A:HOH507 4.3 31.4 1.0 HB3 B:HIS1 4.4 13.0 1.0 CE1 B:TYR168 4.4 11.6 1.0 C B:HIS1 4.4 13.8 1.0 D1 A:HOH507 4.4 22.6 1.0 HE1 B:HIS157 4.6 17.3 1.0 CE2 B:TYR168 4.6 10.3 1.0 HE2 B:TYR168 4.6 9.6 1.0 O B:HOH582 4.7 48.0 1.0 HG3 B:MET80 4.7 9.3 1.0 D1 B:HOH582 4.7 22.3 1.0 D2 B:HOH476 4.7 12.9 1.0 O B:HIS1 4.8 12.2 1.0 CD B:GLN166 4.9 19.5 1.0 D2 B:HOH582 5.0 27.4 1.0 DE2 B:HIS1 5.0 16.5 1.0 HE22 B:GLN166 5.0 19.8 0.0

G.C.Schroder, W.B.O'dell, S.P.Webb, P.K.Agarwal, F.Meilleur. Capture of Activated Dioxygen Intermediates at the Copper-Active Site of A Lytic Polysaccharide Monooxygenase. Chem Sci V. 13 13303 2022.
ISSN: ISSN 2041-6520
PubMed: 36507176
DOI: 10.1039/D2SC05031E