Copper in PDB 7pxt: Structure of An Lpmo, Collected From Serial Synchrotron Crystallography Data.

All present enzymatic activity of Structure of An Lpmo, Collected From Serial Synchrotron Crystallography Data.:
1.14.99.56;

The structure of Structure of An Lpmo, Collected From Serial Synchrotron Crystallography Data., PDB code: 7pxt was solved by T.Tandrup, G.Santoni, L.Lo Leggio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.69 / 2.40
Space group	P 41 3 2
Cell size a, b, c (Å), α, β, γ (°)	125.42, 125.42, 125.42, 90, 90, 90
R / Rfree (%)	18.7 / 24.8

The binding sites of Copper atom in the Structure of An Lpmo, Collected From Serial Synchrotron Crystallography Data. (pdb code 7pxt). 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, Collected From Serial Synchrotron Crystallography Data., PDB code: 7pxt:

Copper binding site 1 out of 1 in the Structure of An Lpmo, Collected From Serial Synchrotron Crystallography Data.


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, Collected From Serial Synchrotron Crystallography Data. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:22.2 occ:1.00 ND1 A:HIC1 1.9 22.1 1.0 NE2 A:HIS78 1.9 21.0 1.0 N A:HIC1 2.2 20.2 1.0 OH A:TYR164 2.7 13.1 1.0 CE1 A:HIC1 2.8 21.6 1.0 O A:HOH520 2.9 19.6 1.0 CD2 A:HIS78 2.9 20.7 1.0 CE1 A:HIS78 2.9 20.9 1.0 CG A:HIC1 3.0 21.1 1.0 CA A:HIC1 3.3 19.6 1.0 CB A:HIC1 3.5 20.1 1.0 CZ A:TYR164 3.7 12.9 1.0 OE1 A:GLN162 3.7 18.2 1.0 O A:HOH564 3.9 30.6 1.0 NE2 A:HIC1 4.0 22.0 1.0 ND1 A:HIS78 4.0 20.9 1.0 CG A:HIS78 4.0 20.9 1.0 CD2 A:HIC1 4.1 21.8 1.0 O A:HOH460 4.2 17.7 1.0 CE1 A:TYR164 4.3 13.3 1.0 CE2 A:TYR164 4.5 12.5 1.0 C A:HIC1 4.6 18.4 1.0 CD A:GLN162 4.8 17.7 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