Atomistry » Copper » PDB 4mfh-4rkn » 4opb
Atomistry »
  Copper »
    PDB 4mfh-4rkn »
      4opb »

Copper in PDB 4opb: AA13 Lytic Polysaccharide Monooxygenase From Aspergillus Oryzae

Protein crystallography data

The structure of AA13 Lytic Polysaccharide Monooxygenase From Aspergillus Oryzae, PDB code: 4opb was solved by L.Lo Leggio, K.H.Frandsen, G.J.Davies, P.Dupree, P.Walton, B.Henrissat, M.Stringer, M.Tovborg, L.De Maria, K.S.Johansen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.560, 61.600, 73.160, 90.00, 90.00, 90.00
R / Rfree (%) 11.9 / 17

Other elements in 4opb:

The structure of AA13 Lytic Polysaccharide Monooxygenase From Aspergillus Oryzae also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Copper Binding Sites:

The binding sites of Copper atom in the AA13 Lytic Polysaccharide Monooxygenase From Aspergillus Oryzae (pdb code 4opb). 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 AA13 Lytic Polysaccharide Monooxygenase From Aspergillus Oryzae, PDB code: 4opb:

Copper binding site 1 out of 1 in 4opb

Go back to Copper Binding Sites List in 4opb
Copper binding site 1 out of 1 in the AA13 Lytic Polysaccharide Monooxygenase From Aspergillus Oryzae


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of AA13 Lytic Polysaccharide Monooxygenase From Aspergillus Oryzae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:10.6
occ:1.00
ND1 A:HIC1 1.9 9.9 1.0
NE2 A:HIS91 2.0 9.3 1.0
N A:HIC1 2.2 10.2 1.0
OH A:TYR224 2.5 11.5 1.0
CE1 A:HIC1 2.9 10.7 1.0
CG A:HIC1 2.9 9.6 1.0
CD2 A:HIS91 3.0 9.7 1.0
CE1 A:HIS91 3.0 11.2 1.0
CA A:HIC1 3.2 8.7 1.0
CB A:HIC1 3.3 11.2 1.0
CZ A:TYR224 3.5 9.9 1.0
O A:HOH592 3.6 30.3 1.0
O A:GLY89 3.8 9.2 1.0
OE1 A:GLN222 3.9 11.8 1.0
O A:HOH591 3.9 38.5 1.0
CA A:GLY89 3.9 9.7 1.0
NE2 A:HIC1 4.0 10.7 1.0
CD2 A:HIC1 4.1 8.5 1.0
ND1 A:HIS91 4.1 10.7 1.0
CG A:HIS91 4.1 7.5 1.0
CE2 A:TYR224 4.2 9.7 1.0
C A:GLY89 4.3 9.0 1.0
CE1 A:TYR224 4.4 10.1 1.0
C A:HIC1 4.5 8.7 1.0
O A:HOH403 4.6 19.2 1.0
CD A:GLN222 4.7 11.3 1.0
CD1 A:ILE27 4.8 19.9 1.0
NE2 A:GLN222 4.9 19.1 1.0
O A:HIC1 5.0 9.2 1.0

Reference:

L.Lo Leggio, T.J.Simmons, J.C.N.Poulsen, K.E.H.Frandsen, G.R.Hemsworth, M.A.Stringer, P.Von Freiesleben, M.Tovborg, K.S.Johansen, L.De Maria, P.V.Harris, C.L.Soong, P.Dupree, T.Tryfona, N.Lenfant, B.Henrissat, G.J.Davies, P.H.Walton. Structure and Boosting Activity of A Starch-Degrading Lytic Polysaccharide Monooxygenase. Nat Commun 2015.
ISSN: ESSN 2041-1723
DOI: NCOMMS6961
Page generated: Mon Jul 14 03:58:25 2025

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy