Chlorine in PDB 7pyf: Structure of Lpmo in Complex with Cellotetraose at 1.39X10^5 Gy

The structure of Structure of Lpmo in Complex with Cellotetraose at 1.39X10^5 Gy, PDB code: 7pyf 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)	44.45 / 1.90
Space group	P 41 3 2
Cell size a, b, c (Å), α, β, γ (°)	125.62, 125.62, 125.62, 90, 90, 90
R / Rfree (%)	25.4 / 28.7

The structure of Structure of Lpmo in Complex with Cellotetraose at 1.39X10^5 Gy also contains other interesting chemical elements:

Copper

(Cu)

1 atom

The binding sites of Chlorine atom in the Structure of Lpmo in Complex with Cellotetraose at 1.39X10^5 Gy (pdb code 7pyf). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Structure of Lpmo in Complex with Cellotetraose at 1.39X10^5 Gy, PDB code: 7pyf:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Structure of Lpmo in Complex with Cellotetraose at 1.39X10^5 Gy


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Lpmo in Complex with Cellotetraose at 1.39X10^5 Gy within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:45.6 occ:0.90 CL A:CL303 0.0 45.6 0.9 CL A:CL303 2.0 5.8 0.1 NE2 A:HIS147 3.2 48.5 1.0 NE2 A:GLN162 3.2 37.1 1.0 C1 B:BGC3 3.5 35.5 1.0 C5 B:BGC3 3.8 40.1 1.0 CE1 A:HIC1 3.8 31.8 1.0 O5 B:BGC3 3.8 40.0 1.0 CU A:CU301 3.9 37.9 1.0 OE1 A:GLN162 4.0 37.1 1.0 NE2 A:HIS78 4.0 44.0 1.0 CD2 A:HIS147 4.0 47.7 1.0 C4 B:BGC2 4.0 39.3 1.0 CE1 A:HIS78 4.0 46.8 1.0 CD A:GLN162 4.0 39.4 1.0 O A:HOH485 4.1 37.1 1.0 O3 B:BGC2 4.1 39.0 1.0 ND1 A:HIC1 4.2 32.1 1.0 O4 B:BGC2 4.3 35.9 1.0 CE1 A:HIS147 4.3 49.5 1.0 C3 B:BGC3 4.4 37.4 1.0 C2 B:BGC3 4.5 38.8 1.0 C4 B:BGC3 4.6 40.9 1.0 C3 B:BGC2 4.7 41.4 1.0 O6 B:BGC3 4.7 51.4 1.0 OE1 A:GLU148 4.8 41.2 1.0 O4 B:BGC3 4.8 39.5 1.0 C6 B:BGC3 4.8 43.2 1.0 OH A:TYR164 4.9 21.4 1.0 NE2 A:HIC1 5.0 32.5 1.0

Chlorine binding site 2 out of 3 in the Structure of Lpmo in Complex with Cellotetraose at 1.39X10^5 Gy


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Lpmo in Complex with Cellotetraose at 1.39X10^5 Gy within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:5.8 occ:0.10 CL A:CL303 0.0 5.8 0.1 CU A:CU301 1.9 37.9 1.0 CL A:CL303 2.0 45.6 0.9 NE2 A:HIS78 2.3 44.0 1.0 CE1 A:HIS78 2.8 46.8 1.0 ND1 A:HIC1 2.9 32.1 1.0 CE1 A:HIC1 3.1 31.8 1.0 OE1 A:GLN162 3.2 37.1 1.0 NE2 A:HIS147 3.3 48.5 1.0 OH A:TYR164 3.4 21.4 1.0 CD2 A:HIS78 3.4 44.2 1.0 NE2 A:GLN162 3.7 37.1 1.0 CD A:GLN162 3.8 39.4 1.0 CE1 A:HIS147 3.9 49.5 1.0 N A:HIC1 4.0 39.0 1.0 ND1 A:HIS78 4.0 43.2 1.0 C6 B:BGC2 4.1 40.8 1.0 C4 B:BGC2 4.2 39.3 1.0 C1 B:BGC3 4.2 35.5 1.0 CG A:HIC1 4.3 36.6 1.0 CG A:HIS78 4.3 41.9 1.0 CD2 A:HIS147 4.4 47.7 1.0 NE2 A:HIC1 4.4 32.5 1.0 O4 B:BGC2 4.6 35.9 1.0 CZ A:TYR164 4.6 28.7 1.0 C5 B:BGC2 4.7 42.6 1.0 O A:HOH485 4.9 37.1 1.0 O2 B:BGC3 5.0 45.7 1.0

Chlorine binding site 3 out of 3 in the Structure of Lpmo in Complex with Cellotetraose at 1.39X10^5 Gy


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of Lpmo in Complex with Cellotetraose at 1.39X10^5 Gy within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:14.4 occ:0.20 O A:HOH415 1.1 33.5 0.8 O A:SER175 1.9 43.0 0.2 O A:HOH411 2.4 41.1 1.0 OD2 A:ASP176 2.9 34.6 0.2 C A:SER175 3.0 39.3 0.2 CG A:ASP176 3.0 36.2 0.2 N A:ASP176 3.1 43.9 0.8 OD1 A:ASP176 3.3 34.1 0.2 CA A:SER175 3.5 34.7 0.8 CA A:SER175 3.6 37.9 0.2 ND1 A:HIS131 3.6 44.8 1.0 C A:SER175 3.7 39.0 0.8 CB A:ASP176 3.8 37.0 0.2 CG A:ASP176 3.9 42.6 0.8 CE1 A:HIS131 3.9 43.8 1.0 CB A:ALA56 4.0 34.0 1.0 CB A:ASP176 4.1 42.3 0.8 N A:ASP176 4.1 39.2 0.2 OD1 A:ASP176 4.1 41.7 0.8 CA A:ASP176 4.2 44.1 0.8 OD2 A:ASP176 4.2 37.9 0.8 N A:SER175 4.2 37.7 0.2 N A:SER175 4.3 35.4 0.8 O A:HOH477 4.4 44.5 1.0 CB A:SER175 4.4 35.0 0.8 OG A:SER175 4.5 30.1 0.8 CA A:ASP176 4.6 38.8 0.2 O A:SER174 4.6 37.1 1.0 C A:SER174 4.6 38.0 1.0 OG A:SER174 4.7 40.8 0.5 CG A:HIS131 4.8 40.9 1.0 O A:SER175 4.9 43.0 0.8 CB A:SER175 5.0 37.5 0.2

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