Copper in PDB 9exj: Crystal Structure of Aspergillus Fumigatus AA11 Lytic Polysaccharide Monooxygenase (AFAA11B) in Complex with Cu(II)

The structure of Crystal Structure of Aspergillus Fumigatus AA11 Lytic Polysaccharide Monooxygenase (AFAA11B) in Complex with Cu(II), PDB code: 9exj was solved by K.R.Hall, S.E.Ronnekleiv, R.Skaali, L.Rieder, A.N.B.Englund, E.L.Dalleywater, I.Ayuso-Fernandez, O.Golten, A.K.Rohr, M.Sorlie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.05 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.414, 53.777, 71.834, 90, 90, 90
R / Rfree (%)	15.1 / 19.1

The binding sites of Copper atom in the Crystal Structure of Aspergillus Fumigatus AA11 Lytic Polysaccharide Monooxygenase (AFAA11B) in Complex with Cu(II) (pdb code 9exj). 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 Crystal Structure of Aspergillus Fumigatus AA11 Lytic Polysaccharide Monooxygenase (AFAA11B) in Complex with Cu(II), PDB code: 9exj:

Copper binding site 1 out of 1 in the Crystal Structure of Aspergillus Fumigatus AA11 Lytic Polysaccharide Monooxygenase (AFAA11B) in Complex with Cu(II)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Aspergillus Fumigatus AA11 Lytic Polysaccharide Monooxygenase (AFAA11B) in Complex with Cu(II) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu303 b:14.1 occ:1.00 ND1 A:HIS26 2.0 12.9 1.0 NE2 A:HIS86 2.0 12.7 1.0 N A:HIS26 2.2 11.4 1.0 O A:HOH564 2.5 26.8 1.0 OH A:TYR166 2.6 12.1 1.0 O A:HOH577 2.9 28.4 1.0 CG A:HIS26 3.0 12.3 1.0 CE1 A:HIS86 3.0 15.1 1.0 CD2 A:HIS86 3.0 13.4 1.0 CE1 A:HIS26 3.0 14.3 1.0 CA A:HIS26 3.2 10.2 1.0 CB A:HIS26 3.3 12.2 1.0 CZ A:TYR166 3.8 9.9 1.0 ND1 A:HIS86 4.1 16.2 1.0 CD2 A:HIS26 4.1 12.9 1.0 NE2 A:HIS26 4.1 14.3 1.0 CG A:HIS86 4.1 13.3 1.0 CB A:ALA84 4.3 12.9 1.0 CE2 A:TYR166 4.3 9.0 1.0 O A:ALA84 4.4 11.1 1.0 C A:HIS26 4.5 9.9 1.0 OE1 A:GLU164 4.6 21.7 0.5 O A:HOH425 4.7 33.7 1.0 O A:HOH608 4.8 28.8 1.0 CE1 A:TYR166 4.8 9.4 1.0

K.R.Hall, S.E.Ronnekleiv, R.Skaali, L.Rieder, A.N.B.Englund, E.L.Dalleywater, I.Ayuso-Fernandez, O.Golten, A.K.Rohr, M.Sorlie. Surface Topology Prevents Efficient Chitin Degradation For A Clade of Lpmos To Be Published.