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Copper in PDB 7pyz: Structure of Lpmo (Expressed in E.Coli) with Cellotriose at 2.97X10^6 Gy

Protein crystallography data

The structure of Structure of Lpmo (Expressed in E.Coli) with Cellotriose at 2.97X10^6 Gy, PDB code: 7pyz was solved by T.Tandrup, S.J.Muderspach, S.Banerjee, J.O.Ipsen, C.H.Rollan, M.H.H.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) 34.57 / 1.60
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 48.85, 48.85, 108.78, 90, 90, 90
R / Rfree (%) 12.3 / 14.4

Other elements in 7pyz:

The structure of Structure of Lpmo (Expressed in E.Coli) with Cellotriose at 2.97X10^6 Gy also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Structure of Lpmo (Expressed in E.Coli) with Cellotriose at 2.97X10^6 Gy (pdb code 7pyz). 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 Lpmo (Expressed in E.Coli) with Cellotriose at 2.97X10^6 Gy, PDB code: 7pyz:

Copper binding site 1 out of 1 in 7pyz

Go back to Copper Binding Sites List in 7pyz
Copper binding site 1 out of 1 in the Structure of Lpmo (Expressed in E.Coli) with Cellotriose at 2.97X10^6 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 Lpmo (Expressed in E.Coli) with Cellotriose at 2.97X10^6 Gy within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:8.5
occ:0.90
ND1 A:HIS1 1.9 9.5 1.0
NE2 A:HIS78 2.0 8.8 1.0
N A:HIS1 2.3 9.6 1.0
OH A:TYR164 2.7 9.0 1.0
CE1 A:HIS1 2.9 9.1 1.0
CD2 A:HIS78 2.9 8.3 1.0
CG A:HIS1 3.0 9.2 1.0
CE1 A:HIS78 3.0 8.6 1.0
CA A:HIS1 3.2 8.5 1.0
CB A:HIS1 3.4 8.8 1.0
C6 C:BGC2 3.6 14.9 1.0
CL A:CL302 3.6 32.3 1.0
CZ A:TYR164 3.7 7.8 1.0
OE1 A:GLN162 3.9 11.2 1.0
NE2 A:HIS1 4.1 10.4 1.0
CG A:HIS78 4.1 8.7 1.0
CD2 A:HIS1 4.1 9.1 1.0
ND1 A:HIS78 4.1 8.8 1.0
O A:HOH525 4.1 10.2 1.0
CE1 A:TYR164 4.3 7.0 1.0
O6 C:BGC2 4.4 15.7 1.0
CE2 A:TYR164 4.5 7.3 1.0
O5 C:BGC2 4.5 15.8 1.0
C5 C:BGC2 4.5 17.7 1.0
C A:HIS1 4.6 8.9 1.0
C4 C:BGC2 4.7 20.7 1.0
CD A:GLN162 4.8 10.9 1.0
O A:HOH637 4.8 27.7 1.0

Reference:

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
Page generated: Wed Jul 31 09:00:14 2024

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