Copper in PDB 7pxw: Lpmo, Expressed in E.Coli, in Complex with Cellotetraose

The structure of Lpmo, Expressed in E.Coli, in Complex with Cellotetraose, PDB code: 7pxw was solved by S.Banerjee, S.J.Muderspach, T.Tandrup, J.Ipsen, C.H.Rollan, M.Norholm, 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)	44.58 / 1.40
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	48.77, 48.77, 109.32, 90, 90, 90
R / Rfree (%)	11.7 / 16

The structure of Lpmo, Expressed in E.Coli, in Complex with Cellotetraose also contains other interesting chemical elements:

Chlorine

(Cl)

19 atoms

The binding sites of Copper atom in the Lpmo, Expressed in E.Coli, in Complex with Cellotetraose (pdb code 7pxw). 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 Lpmo, Expressed in E.Coli, in Complex with Cellotetraose, PDB code: 7pxw:

Copper binding site 1 out of 1 in the Lpmo, Expressed in E.Coli, in Complex with Cellotetraose


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Lpmo, Expressed in E.Coli, in Complex with Cellotetraose within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu403 b:18.4 occ:0.90 ND1 A:HIS1 1.9 20.4 1.0 NE2 A:HIS78 2.0 19.2 1.0 O A:HOH610 2.3 33.9 0.6 N A:HIS1 2.3 18.0 1.0 OH A:TYR164 2.7 19.1 1.0 CE1 A:HIS1 2.9 20.9 1.0 CD2 A:HIS78 2.9 18.4 1.0 CG A:HIS1 3.0 19.7 1.0 CE1 A:HIS78 3.0 20.9 1.0 CA A:HIS1 3.3 18.3 1.0 CB A:HIS1 3.3 18.9 1.0 C6 C:BGC3 3.6 23.6 1.0 CZ A:TYR164 3.7 16.5 1.0 OE1 A:GLN162 3.8 20.8 1.0 CL A:CL419 3.9 25.8 0.6 NE2 A:HIS1 4.1 21.8 1.0 CD2 A:HIS1 4.1 21.9 1.0 ND1 A:HIS78 4.1 18.6 1.0 CG A:HIS78 4.1 18.2 1.0 O A:HOH626 4.1 21.0 1.0 CE1 A:TYR164 4.3 17.0 1.0 O6 C:BGC3 4.3 26.6 1.0 C5 C:BGC3 4.5 20.8 0.5 CE2 A:TYR164 4.5 16.2 1.0 C4 C:BGC3 4.5 20.7 0.5 O5 C:BGC3 4.5 22.6 0.8 C A:HIS1 4.6 18.7 1.0 CD A:GLN162 4.8 19.7 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