Copper in PDB 7pxi: X-Ray Structure of Lpmo at 7.88X10^3 Gy

All present enzymatic activity of X-Ray Structure of Lpmo at 7.88X10^3 Gy:
1.14.99.56;

The structure of X-Ray Structure of Lpmo at 7.88X10^3 Gy, PDB code: 7pxi 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)	44.23 / 1.63
Space group	P 41 3 2
Cell size a, b, c (Å), α, β, γ (°)	124.98, 124.98, 124.98, 90, 90, 90
R / Rfree (%)	18.3 / 21

The binding sites of Copper atom in the X-Ray Structure of Lpmo at 7.88X10^3 Gy (pdb code 7pxi). 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 7.88X10^3 Gy, PDB code: 7pxi:

Copper binding site 1 out of 1 in the X-Ray Structure of Lpmo at 7.88X10^3 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 7.88X10^3 Gy within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:16.0 occ:1.00 ND1 A:HIC1 1.9 15.2 1.0 NE2 A:HIS78 2.0 14.8 1.0 O A:HOH522 2.2 15.8 1.0 N A:HIC1 2.2 14.7 1.0 O A:HOH616 2.7 12.8 1.0 OH A:TYR164 2.7 14.6 1.0 CE1 A:HIC1 2.9 16.1 1.0 CG A:HIC1 2.9 15.2 1.0 CE1 A:HIS78 3.0 16.6 1.0 CD2 A:HIS78 3.0 13.9 1.0 CA A:HIC1 3.1 13.9 1.0 CB A:HIC1 3.3 14.4 1.0 CZ A:TYR164 3.7 14.6 1.0 OE1 A:GLN162 3.8 16.6 1.0 NE2 A:HIC1 4.0 16.6 1.0 CD2 A:HIC1 4.1 16.0 1.0 O A:HOH500 4.1 17.3 1.0 ND1 A:HIS78 4.1 15.5 1.0 O A:HOH606 4.1 40.1 1.0 CG A:HIS78 4.1 15.2 1.0 CE1 A:TYR164 4.4 14.2 1.0 C A:HIC1 4.5 14.6 1.0 CE2 A:TYR164 4.6 14.1 1.0 O A:HIC1 4.9 16.5 1.0 CD A:GLN162 4.9 17.2 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