Copper in PDB 7pxr: Room Temperature Structure of An Lpmo.

All present enzymatic activity of Room Temperature Structure of An Lpmo.:
1.14.99.56;

The structure of Room Temperature Structure of An Lpmo., PDB code: 7pxr was solved by T.Tandrup, F.Meilleur, J.Ipsen, K.S.Johansen, L.Lo Leggio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.87 / 1.80
Space group	P 41 3 2
Cell size a, b, c (Å), α, β, γ (°)	126.659, 126.659, 126.659, 90, 90, 90
R / Rfree (%)	14.7 / 16.6

The structure of Room Temperature Structure of An Lpmo. also contains other interesting chemical elements:

Chlorine

(Cl)

13 atoms

The binding sites of Copper atom in the Room Temperature Structure of An Lpmo. (pdb code 7pxr). 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 Room Temperature Structure of An Lpmo., PDB code: 7pxr:

Copper binding site 1 out of 1 in the Room Temperature Structure of An Lpmo.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Room Temperature Structure of An Lpmo. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:18.8 occ:1.00 ND1 A:HIC1 1.9 18.1 1.0 NE2 A:HIS78 2.0 19.9 1.0 N A:HIC1 2.2 15.2 1.0 O A:HOH506 2.2 15.5 1.0 CL A:CL303 2.8 27.1 0.8 OH A:TYR164 2.8 17.0 1.0 CE1 A:HIC1 2.9 18.3 1.0 CG A:HIC1 3.0 18.0 1.0 CE1 A:HIS78 3.0 21.5 1.0 CD2 A:HIS78 3.1 19.5 1.0 CA A:HIC1 3.2 15.2 1.0 CB A:HIC1 3.4 16.3 1.0 CZ A:TYR164 3.8 16.4 1.0 OE1 A:GLN162 3.9 18.4 1.0 NE2 A:HIC1 4.0 20.3 1.0 O A:HOH484 4.1 22.4 1.0 CD2 A:HIC1 4.1 19.4 1.0 ND1 A:HIS78 4.2 20.6 1.0 CG A:HIS78 4.2 18.0 1.0 CE1 A:TYR164 4.4 15.1 1.0 C A:HIC1 4.5 13.6 1.0 CE2 A:TYR164 4.7 15.8 1.0 O A:HOH523 4.8 33.6 1.0 O A:HOH534 4.9 50.8 1.0 O A:HIC1 4.9 16.5 1.0 CD A:GLN162 5.0 19.2 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