Copper in PDB 5nns: Crystal Structure of HILPMO9B

The structure of Crystal Structure of HILPMO9B, PDB code: 5nns was solved by M.Dimarogona, M.Sandgren, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.38 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	53.695, 46.375, 86.492, 90.00, 103.23, 90.00
R / Rfree (%)	20 / 25.1

The structure of Crystal Structure of HILPMO9B also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Copper atom in the Crystal Structure of HILPMO9B (pdb code 5nns). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of HILPMO9B, PDB code: 5nns:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of HILPMO9B


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 HILPMO9B within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu303 b:20.8 occ:1.00 NE2 A:HIS80 2.1 11.9 1.0 ND1 A:HIS1 2.2 18.4 1.0 N A:HIS1 2.4 16.5 1.0 OH A:TYR167 2.9 11.8 1.0 CD2 A:HIS80 3.0 11.9 1.0 CG A:HIS1 3.0 17.9 1.0 O2 A:GOL309 3.1 13.8 0.5 CA A:HIS1 3.2 16.4 1.0 CE1 A:HIS80 3.2 12.1 1.0 CB A:HIS1 3.2 17.2 1.0 CE1 A:HIS1 3.2 18.7 1.0 CZ A:TYR167 4.0 11.7 1.0 OE1 A:GLN165 4.1 13.5 1.0 CG A:HIS80 4.2 11.9 1.0 CD2 A:HIS1 4.2 18.6 1.0 ND1 A:HIS80 4.3 12.1 1.0 NE2 A:HIS1 4.3 18.6 1.0 C2 A:GOL309 4.3 13.7 0.5 CG A:PRO79 4.5 11.8 1.0 C A:HIS1 4.6 15.7 1.0 CE1 A:TYR167 4.7 11.8 1.0 CE2 A:TYR167 4.8 11.7 1.0

Copper binding site 2 out of 2 in the Crystal Structure of HILPMO9B


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of HILPMO9B within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu303 b:21.0 occ:1.00 NE2 B:HIS80 2.1 14.3 1.0 ND1 B:HIS1 2.1 15.2 1.0 N B:HIS1 2.5 14.6 1.0 O1 B:GOL309 2.7 16.9 0.5 OH B:TYR167 2.8 11.8 1.0 CD2 B:HIS80 2.9 14.3 1.0 CG B:HIS1 3.0 15.0 1.0 O2 B:GOL310 3.1 24.5 1.0 CE1 B:HIS80 3.1 14.4 1.0 CE1 B:HIS1 3.2 15.5 1.0 CA B:HIS1 3.2 14.6 1.0 CB B:HIS1 3.3 14.8 1.0 C1 B:GOL309 3.6 16.8 0.5 CZ B:TYR167 3.9 12.0 1.0 OE1 B:GLN165 4.0 12.4 1.0 CG B:HIS80 4.1 14.2 1.0 C2 B:GOL310 4.2 24.0 1.0 CD2 B:HIS1 4.2 15.2 1.0 ND1 B:HIS80 4.2 14.1 1.0 NE2 B:HIS1 4.2 15.3 1.0 CE1 B:TYR167 4.5 11.9 1.0 CG B:PRO79 4.5 13.6 1.0 C B:HIS1 4.6 14.1 1.0 O3 B:GOL310 4.7 24.2 1.0 C3 B:GOL310 4.8 24.4 1.0 CE2 B:TYR167 4.8 11.8 1.0 C2 B:GOL309 4.9 16.9 0.5 CE1 B:HIS159 5.0 12.7 1.0 O2 B:GOL309 5.0 17.0 0.5

B.Liu, A.A.Kognole, M.Wu, B.Westereng, M.F.Crowley, S.Kim, M.Dimarogona, C.M.Payne, M.Sandgren. Structural and Molecular Dynamics Studies of A C1-Oxidizing Lytic Polysaccharide Monooxygenase From Heterobasidion Irregulare Reveal Amino Acids Important For Substrate Recognition. Febs J. V. 285 2225 2018.
ISSN: ISSN 1742-4658
PubMed: 29660793
DOI: 10.1111/FEBS.14472