Copper in PDB 5ftz: AA10 Lytic Polysaccharide Monooxygenase (Lpmo) From Streptomyces Lividans

The structure of AA10 Lytic Polysaccharide Monooxygenase (Lpmo) From Streptomyces Lividans, PDB code: 5ftz was solved by A.K.C.Chaplin, M.T.Wilson, M.A.Hough, D.A.Svistunenko, G.R.Hemsworth, P.H.Walton, E.Vijgenboom, J.A.R.Worrall, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.76 / 1.38
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	69.620, 32.430, 61.320, 90.00, 97.77, 90.00
R / Rfree (%)	13.504 / 15.999

The binding sites of Copper atom in the AA10 Lytic Polysaccharide Monooxygenase (Lpmo) From Streptomyces Lividans (pdb code 5ftz). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the AA10 Lytic Polysaccharide Monooxygenase (Lpmo) From Streptomyces Lividans, PDB code: 5ftz:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the AA10 Lytic Polysaccharide Monooxygenase (Lpmo) From Streptomyces Lividans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of AA10 Lytic Polysaccharide Monooxygenase (Lpmo) From Streptomyces Lividans within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu202 b:14.5 occ:0.80 NE2 A:HIS120 1.9 19.6 1.0 ND1 A:HIS30 1.9 14.7 1.0 N A:HIS30 2.2 12.6 1.0 CD2 A:HIS120 2.8 17.8 1.0 CE1 A:HIS30 2.9 16.3 1.0 CG A:HIS30 2.9 13.4 1.0 CE1 A:HIS120 2.9 22.4 1.0 CA A:HIS30 3.2 11.3 1.0 CB A:HIS30 3.3 12.3 1.0 CZ A:PHE193 3.6 11.9 1.0 CB A:ALA118 3.8 21.4 1.0 NE2 A:HIS30 4.0 16.1 1.0 CG A:HIS120 4.0 17.7 1.0 ND1 A:HIS120 4.0 21.1 1.0 CD2 A:HIS30 4.0 15.2 1.0 CE1 A:PHE193 4.0 11.3 1.0 O A:ALA118 4.3 18.5 1.0 O A:HOH2057 4.4 39.8 1.0 CE2 A:PHE193 4.4 11.1 1.0 C A:HIS30 4.5 10.4 1.0 CA A:ALA118 4.9 19.4 1.0 O A:HIS30 4.9 11.1 1.0 C A:ALA118 5.0 19.0 1.0

Copper binding site 2 out of 2 in the AA10 Lytic Polysaccharide Monooxygenase (Lpmo) From Streptomyces Lividans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of AA10 Lytic Polysaccharide Monooxygenase (Lpmo) From Streptomyces Lividans within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu203 b:12.6 occ:0.50 NE2 A:HIS187 1.9 10.0 1.0 OD2 A:ASP188 2.4 16.9 1.0 CE1 A:HIS187 2.8 12.1 1.0 CD2 A:HIS187 3.0 10.9 1.0 CG A:ASP188 3.2 12.3 1.0 OD1 A:ASP188 3.5 13.3 1.0 O A:HOH2227 3.6 16.3 0.5 O A:HOH2228 3.9 29.4 1.0 ND1 A:HIS187 4.0 12.8 1.0 CG A:HIS187 4.1 10.7 1.0 CB A:ASP188 4.4 11.6 1.0 O A:HOH2114 4.7 29.9 1.0

A.K.Chaplin, M.T.Wilson, M.A.Hough, D.A.Svistunenko, G.R.Hemsworth, P.H.Walton, E.Vijgenboom, J.A.R.Worrall. Heterogeneity in the Histidine-Brace Copper Coordination Sphere in AA10 Lytic Polysaccharide Monooxygenases. J.Biol.Chem. V. 291 12838 2016.
ISSN: ISSN 0021-9258
PubMed: 27129229
DOI: 10.1074/JBC.M116.722447