Copper in PDB 4qi8: Lytic Polysaccharide Monooxygenase 9F From Neurospora Crassa, NCLPMO9F

The structure of Lytic Polysaccharide Monooxygenase 9F From Neurospora Crassa, NCLPMO9F, PDB code: 4qi8 was solved by T.C.Tan, R.Gandini, C.Sygmund, R.Kittl, D.Haltrich, R.Ludwig, B.M.Hallberg, C.Divne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.22 / 1.10
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	71.730, 162.490, 32.999, 90.00, 90.00, 90.00
R / Rfree (%)	13.1 / 14.9

The binding sites of Copper atom in the Lytic Polysaccharide Monooxygenase 9F From Neurospora Crassa, NCLPMO9F (pdb code 4qi8). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Lytic Polysaccharide Monooxygenase 9F From Neurospora Crassa, NCLPMO9F, PDB code: 4qi8:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Lytic Polysaccharide Monooxygenase 9F From Neurospora Crassa, NCLPMO9F


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Lytic Polysaccharide Monooxygenase 9F From Neurospora Crassa, NCLPMO9F within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:6.7 occ:1.00 ND1 A:HIS1 2.0 7.8 1.0 NE2 A:HIS72 2.0 7.2 1.0 O A:HOH689 2.0 10.4 1.0 N A:HIS1 2.1 6.8 1.0 O A:HOH452 2.5 11.5 1.0 OH A:TYR157 2.6 5.8 1.0 HH A:TYR157 2.8 6.9 1.0 CE1 A:HIS72 2.9 7.3 1.0 CE1 A:HIS1 3.0 10.7 1.0 CG A:HIS1 3.0 7.3 1.0 CD2 A:HIS72 3.0 5.7 1.0 CA A:HIS1 3.1 5.9 1.0 HE1 A:HIS72 3.1 8.7 1.0 HE1 A:HIS1 3.2 12.9 1.0 HA A:HIS1 3.2 7.1 1.0 HD2 A:HIS72 3.3 6.9 1.0 CB A:HIS1 3.3 6.3 1.0 HB2 A:HIS1 3.4 7.6 1.0 CZ A:TYR157 3.7 5.5 1.0 OH A:TYR71 3.7 10.6 1.0 OE1 A:GLN155 3.9 6.5 1.0 HH A:TYR71 3.9 12.8 1.0 HE1 A:TYR157 4.0 6.3 1.0 O A:HOH608 4.0 21.6 1.0 ND1 A:HIS72 4.1 7.4 1.0 NE2 A:HIS1 4.1 12.5 1.0 CD2 A:HIS1 4.1 10.2 1.0 CG A:HIS72 4.2 6.4 1.0 CE1 A:TYR157 4.2 5.2 1.0 CZ A:TYR71 4.3 9.8 1.0 HB3 A:HIS1 4.3 7.6 1.0 HD2 A:PHE31 4.4 6.9 1.0 HE1 A:TYR71 4.4 11.5 1.0 C A:HIS1 4.4 6.1 1.0 O A:HOH629 4.5 15.7 1.0 CE1 A:TYR71 4.6 9.6 1.0 CE2 A:TYR157 4.6 5.2 1.0 HE2 A:TYR157 4.7 6.2 1.0 HE1 A:TYR2 4.7 7.3 1.0 O A:HOH647 4.8 19.8 1.0 HD1 A:HIS72 4.9 8.9 1.0 HE2 A:HIS1 4.9 15.1 1.0 HE2 A:PHE31 5.0 7.0 1.0 HE1 A:HIS146 5.0 10.1 1.0 CD A:GLN155 5.0 5.8 1.0 HD2 A:HIS1 5.0 12.3 1.0

Copper binding site 2 out of 2 in the Lytic Polysaccharide Monooxygenase 9F From Neurospora Crassa, NCLPMO9F


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Lytic Polysaccharide Monooxygenase 9F From Neurospora Crassa, NCLPMO9F within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:5.3 occ:1.00 ND1 B:HIS1 2.0 5.1 1.0 NE2 B:HIS72 2.0 5.2 1.0 N B:HIS1 2.1 5.8 1.0 OD2 A:ASP33 2.2 6.4 1.0 OH B:TYR157 2.6 5.8 1.0 OD1 A:ASP33 2.7 6.4 1.0 HH B:TYR157 2.7 6.9 1.0 CG A:ASP33 2.7 5.9 1.0 CE1 B:HIS72 2.9 5.1 1.0 CE1 B:HIS1 3.0 5.6 1.0 CG B:HIS1 3.0 5.5 1.0 CD2 B:HIS72 3.0 5.0 1.0 CA B:HIS1 3.1 5.3 1.0 HE1 B:HIS72 3.1 6.1 1.0 HE1 B:HIS1 3.2 6.8 1.0 HB2 B:HIS1 3.2 6.5 1.0 HD2 B:HIS72 3.2 6.1 1.0 HH B:TYR71 3.2 7.8 1.0 CB B:HIS1 3.3 5.4 1.0 HA B:HIS1 3.3 6.4 1.0 OH B:TYR71 3.5 6.5 1.0 CZ B:TYR157 3.6 4.7 1.0 OE1 B:GLN155 3.9 7.0 1.0 HE1 B:TYR157 4.0 6.1 1.0 NE2 B:HIS1 4.1 6.3 1.0 ND1 B:HIS72 4.1 5.0 1.0 CD2 B:HIS1 4.1 6.3 1.0 CG B:HIS72 4.1 4.8 1.0 CE1 B:TYR157 4.2 5.1 1.0 HB3 B:HIS1 4.2 6.5 1.0 CB A:ASP33 4.2 5.8 1.0 CZ B:TYR71 4.3 6.3 1.0 HE1 B:TYR71 4.4 8.3 1.0 O A:HOH411 4.4 7.2 1.0 C B:HIS1 4.5 5.4 1.0 HD2 B:PHE31 4.5 7.1 1.0 HE1 A:PHE31 4.5 7.0 1.0 HB3 A:ASP33 4.5 7.0 1.0 CE2 B:TYR157 4.6 4.9 1.0 HE2 B:TYR157 4.6 5.8 1.0 CE1 B:TYR71 4.6 6.9 1.0 HB2 A:ASP33 4.6 7.0 1.0 H A:ASP33 4.7 6.4 1.0 HE2 B:HIS146 4.7 9.4 1.0 HE1 B:TYR2 4.7 6.5 1.0 HE1 B:HIS146 4.8 8.4 1.0 HE2 B:HIS1 4.8 7.6 1.0 HD1 B:HIS72 4.9 6.1 1.0 CD B:GLN155 4.9 6.7 1.0 HD2 B:HIS1 4.9 7.6 1.0 HE22 B:GLN155 5.0 8.2 1.0

T.C.Tan, D.Kracher, R.Gandini, C.Sygmund, R.Kittl, D.Haltrich, B.M.Hallberg, R.Ludwig, C.Divne. Structural Basis For Cellobiose Dehydrogenase Action During Oxidative Cellulose Degradation. Nat Commun V. 6 7542 2015.
ISSN: ESSN 2041-1723
PubMed: 26151670
DOI: 10.1038/NCOMMS8542