Copper in PDB 7pxn: X-Ray Structure of Lpmo at 6.65X10^6 Gy

All present enzymatic activity of X-Ray Structure of Lpmo at 6.65X10^6 Gy:
1.14.99.56;

The structure of X-Ray Structure of Lpmo at 6.65X10^6 Gy, PDB code: 7pxn was solved by T.Tandrup, L.Lo Leggio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.69 / 1.65
Space group	P 41 3 2
Cell size a, b, c (Å), α, β, γ (°)	125.51, 125.51, 125.51, 90, 90, 90
R / Rfree (%)	18 / 20.2

The binding sites of Copper atom in the X-Ray Structure of Lpmo at 6.65X10^6 Gy (pdb code 7pxn). 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 X-Ray Structure of Lpmo at 6.65X10^6 Gy, PDB code: 7pxn:

Copper binding site 1 out of 1 in the X-Ray Structure of Lpmo at 6.65X10^6 Gy


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of X-Ray Structure of Lpmo at 6.65X10^6 Gy within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:32.0 occ:1.00 ND1 A:HIC1 1.9 28.4 1.0 NE2 A:HIS78 2.0 30.5 1.0 N A:HIC1 2.3 26.9 1.0 O A:HOH473 2.6 38.1 0.5 OH A:TYR164 2.7 28.0 1.0 CE1 A:HIC1 2.9 30.2 1.0 CG A:HIC1 3.0 28.5 1.0 CD2 A:HIS78 3.0 29.9 1.0 CE1 A:HIS78 3.0 37.4 1.0 CA A:HIC1 3.2 25.0 1.0 CB A:HIC1 3.3 26.0 1.0 O A:HOH479 3.3 43.4 1.0 CZ A:TYR164 3.7 24.0 1.0 OE1 A:GLN162 3.9 32.8 1.0 NE2 A:HIC1 4.0 32.0 1.0 O A:HOH473 4.1 25.6 0.5 O A:HOH457 4.1 34.0 1.0 CD2 A:HIC1 4.1 31.4 1.0 ND1 A:HIS78 4.1 33.6 1.0 CG A:HIS78 4.1 31.4 1.0 CE1 A:TYR164 4.4 23.7 1.0 CE2 A:TYR164 4.5 21.9 1.0 C A:HIC1 4.5 24.4 1.0 O A:HIC1 5.0 28.2 1.0 CD A:GLN162 5.0 32.5 1.0

T.Tandrup, S.J.Muderspach, S.Banerjee, G.Santoni, J.O.Ipsen, C.Hernandez-Rollan, M.H.H.Norholm, K.S.Johansen, F.Meilleur, L.Lo Leggio. Changes in Active-Site Geometry on X-Ray Photoreduction of A Lytic Polysaccharide Monooxygenase Active-Site Copper and Saccharide Binding. Iucrj V. 9 666 2022.
ISSN: ESSN 2052-2525
PubMed: 36071795
DOI: 10.1107/S2052252522007175