Copper in PDB 5foh: Crystal Structure of the Catalytic Domain of NCLPMO9A

The structure of Crystal Structure of the Catalytic Domain of NCLPMO9A, PDB code: 5foh was solved by B.Westereng, S.K.Kracun, M.Dimarogona, G.Mathiesen, W.G.T.Willats, M.Sandgren, F.L.Aachmann, V.G.H.Eijsink, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	69.64 / 1.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	80.419, 80.419, 57.864, 90.00, 90.00, 120.00
R / Rfree (%)	15.4 / 17.8

The binding sites of Copper atom in the Crystal Structure of the Catalytic Domain of NCLPMO9A (pdb code 5foh). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of the Catalytic Domain of NCLPMO9A, PDB code: 5foh:

Copper binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of NCLPMO9A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of the Catalytic Domain of NCLPMO9A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1226 b:14.6 occ:0.50 ND1 A:HIS1 1.9 23.1 1.0 NE2 A:HIS81 2.2 22.6 1.0 N A:HIS1 2.2 18.4 1.0 OH A:TYR164 2.9 14.1 1.0 CE1 A:HIS1 2.9 23.2 1.0 CG A:HIS1 2.9 21.1 1.0 CD2 A:HIS81 3.0 21.2 1.0 CA A:HIS1 3.1 17.1 1.0 O3 A:SO41227 3.2 55.9 1.0 CE1 A:HIS81 3.2 22.1 1.0 O A:HOH2002 3.3 35.8 1.0 CB A:HIS1 3.3 19.3 1.0 OE1 A:GLN162 3.7 18.3 1.0 CZ A:TYR164 3.9 12.1 1.0 NE2 A:HIS1 4.0 22.9 1.0 CD2 A:HIS1 4.0 22.5 1.0 O A:HOH2001 4.1 27.3 1.0 CG A:HIS81 4.2 20.8 1.0 ND1 A:HIS81 4.3 21.0 1.0 C A:HIS1 4.5 15.8 1.0 CE1 A:TYR164 4.6 11.8 1.0 CE2 A:TYR164 4.6 11.9 1.0 S A:SO41227 4.6 55.4 1.0 CD A:GLN162 4.8 17.1 1.0 O A:HIS1 4.9 15.8 1.0

D.M.Petrovic, A.Varnai, M.Dimarogona, G.Mathiesen, M.Sandgren, B.Westereng, V.G.H.Eijsink. Comparison of Three Seemingly Similar Lytic Polysaccharide Monooxygenases Fromneurospora Crassasuggests Different Roles in Plant Biomass Degradation. J.Biol.Chem. 2019.
ISSN: ESSN 1083-351X
PubMed: 31431506
DOI: 10.1074/JBC.RA119.008196