Copper in PDB 8rry: Crystal Structure of Copper-Loaded SMAA10

The structure of Crystal Structure of Copper-Loaded SMAA10, PDB code: 8rry was solved by A.Munzone, M.Pujol, M.Reglier, A.Royant, A.J.Simaan, C.Decroos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.31 / 1.46
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	53.646, 106.738, 55.459, 90, 99.96, 90
R / Rfree (%)	16 / 18.8

The binding sites of Copper atom in the Crystal Structure of Copper-Loaded SMAA10 (pdb code 8rry). 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 Copper-Loaded SMAA10, PDB code: 8rry:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Copper-Loaded SMAA10


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 Copper-Loaded SMAA10 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:18.9 occ:1.00 NE2 A:HIS114 1.9 20.0 1.0 ND1 A:HIS28 2.0 18.9 1.0 N A:HIS28 2.2 18.2 1.0 CD2 A:HIS114 2.9 19.1 1.0 CE1 A:HIS114 2.9 20.6 1.0 CG A:HIS28 2.9 19.9 1.0 CE1 A:HIS28 3.0 20.3 1.0 CA A:HIS28 3.1 16.9 1.0 CB A:HIS28 3.2 18.8 1.0 O A:HOH456 3.4 31.1 0.5 CZ A:PHE187 3.5 17.9 1.0 CB A:ALA112 3.8 24.4 1.0 ND1 A:HIS114 4.0 19.4 1.0 CG A:HIS114 4.0 18.0 1.0 CD2 A:HIS28 4.1 20.5 1.0 NE2 A:HIS28 4.1 20.0 1.0 CE1 A:PHE187 4.1 17.4 1.0 CE2 A:PHE187 4.3 17.0 1.0 O A:HOH470 4.4 30.0 1.0 O A:ALA112 4.4 23.1 1.0 C A:HIS28 4.4 16.7 1.0 O A:HOH445 4.8 33.6 0.5 O A:HIS28 4.8 15.8 1.0 CA A:ALA112 4.9 22.6 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Copper-Loaded SMAA10


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 Copper-Loaded SMAA10 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu201 b:15.7 occ:1.00 NE2 B:HIS114 2.0 14.7 1.0 ND1 B:HIS28 2.0 14.5 1.0 N B:HIS28 2.2 15.4 1.0 O5 B:CIT203 2.3 18.1 0.2 O4 B:CIT203 2.4 18.1 0.2 O6 B:CIT203 2.5 18.1 0.2 O B:HOH357 2.6 15.7 0.4 O3 B:CIT203 2.6 18.0 0.2 C6 B:CIT203 2.8 17.8 0.2 CG B:HIS28 2.9 15.5 1.0 C5 B:CIT203 2.9 17.8 0.2 CE1 B:HIS114 2.9 17.2 1.0 CD2 B:HIS114 3.0 17.0 1.0 CE1 B:HIS28 3.0 17.3 1.0 CA B:HIS28 3.1 12.7 1.0 CB B:HIS28 3.2 13.9 1.0 CZ B:PHE187 3.6 14.5 1.0 CD2 B:HIS28 4.1 14.3 1.0 ND1 B:HIS114 4.1 16.2 1.0 NE2 B:HIS28 4.1 15.4 1.0 CG B:HIS114 4.1 15.5 1.0 CE1 B:PHE187 4.1 14.5 1.0 CB B:ALA112 4.2 18.5 1.0 C3 B:CIT203 4.3 17.2 0.2 C4 B:CIT203 4.4 17.3 0.2 C B:HIS28 4.4 12.4 1.0 CE2 B:PHE187 4.5 15.3 1.0 O B:ALA112 4.6 18.8 1.0 O7 B:CIT203 4.7 17.2 0.2 O B:HIS28 4.8 14.5 1.0 OE2 B:GLU60 4.8 26.0 1.0 O7 B:CIT203 4.8 17.2 0.2 O2 B:CIT203 4.8 16.3 0.2 C4 B:CIT203 4.9 17.3 0.2 C3 B:CIT203 5.0 17.2 0.2 O B:HOH338 5.0 29.6 1.0

A.Munzone, M.Pujol, A.Tamhankar, C.Joseph, I.Mazurenko, M.Reglier, S.A.V.Jannuzzi, A.Royant, G.Sicoli, S.Debeer, M.Orio, A.J.Simaan, C.Decroos. Integrated Experimental and Theoretical Investigation of Copper Active Site Properties of A Lytic Polysaccharide Monooxygenase From Serratia Marcescens. Inorg.Chem. 2024.
ISSN: ISSN 0020-1669
PubMed: 38814816
DOI: 10.1021/ACS.INORGCHEM.4C00602