Copper in PDB 7pz6: Structure of An Lpmo at 2.22X10^5 Gy

All present enzymatic activity of Structure of An Lpmo at 2.22X10^5 Gy:
3.2.1.4;

The structure of Structure of An Lpmo at 2.22X10^5 Gy, PDB code: 7pz6 was solved by T.Tandrup, S.J.Muderspach, J.O.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)	43.60 / 1.45
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	34.38, 87.21, 37.33, 90, 104.96, 90
R / Rfree (%)	16.9 / 18.9

The binding sites of Copper atom in the Structure of An Lpmo at 2.22X10^5 Gy (pdb code 7pz6). 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 Structure of An Lpmo at 2.22X10^5 Gy, PDB code: 7pz6:

Copper binding site 1 out of 1 in the Structure of An Lpmo at 2.22X10^5 Gy


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of An Lpmo at 2.22X10^5 Gy within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:14.2 occ:1.00 ND1 A:HIC1 1.9 14.6 1.0 NE2 A:HIS86 2.0 10.6 1.0 N A:HIC1 2.2 12.9 1.0 O A:HOH433 2.3 32.0 1.0 O A:HOH401 2.7 31.3 1.0 CD2 A:HIS86 2.9 10.8 1.0 CE1 A:HIC1 2.9 14.5 1.0 CG A:HIC1 2.9 15.0 1.0 OH A:TYR175 3.0 10.9 1.0 CE1 A:HIS86 3.0 10.5 1.0 CA A:HIC1 3.2 13.7 1.0 CB A:HIC1 3.3 14.3 1.0 OE1 A:GLN173 3.9 13.7 1.0 O2S A:EPE304 3.9 19.7 0.6 O A:AKR302 4.0 37.7 1.0 CG A:HIS86 4.0 11.0 1.0 NE2 A:HIC1 4.1 15.1 1.0 ND1 A:HIS86 4.1 10.5 1.0 CD2 A:HIC1 4.1 14.7 1.0 CZ A:TYR175 4.1 11.0 1.0 C A:HIC1 4.5 12.8 1.0 CE2 A:TYR175 4.7 11.3 1.0 O A:HIC1 4.9 13.4 1.0 CG A:PRO83 4.9 13.6 1.0 CE1 A:HIS164 5.0 12.0 1.0 C A:AKR302 5.0 39.8 1.0 CD A:GLN173 5.0 13.9 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