Atomistry » Copper » PDB 1tmx-1x9l » 2cfk
Atomistry »
  Copper »
    PDB 1tmx-1x9l »
      2cfk »

Copper in PDB 2cfk: Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker)

Enzymatic activity of Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker)

All present enzymatic activity of Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker):
1.4.3.6;

Protein crystallography data

The structure of Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker), PDB code: 2cfk was solved by D.B.Langley, A.P.Duff, H.C.Freeman, J.M.Guss, G.A.Juda, D.M.Dooley, S.M.Contakes, N.W.Halpern-Manners, A.R.Dunn, H.B.Gray, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.02 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.885, 62.944, 92.013, 90.00, 112.20, 90.00
R / Rfree (%) 14.5 / 16.5

Copper Binding Sites:

The binding sites of Copper atom in the Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker) (pdb code 2cfk). 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 Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker), PDB code: 2cfk:

Copper binding site 1 out of 1 in 2cfk

Go back to Copper Binding Sites List in 2cfk
Copper binding site 1 out of 1 in the Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Agao in Complex with WC5 (Ru-Wire Inhibitor, 5-Carbon Linker) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1629

b:28.1
occ:1.00
ND1 A:HIS592 2.0 19.5 1.0
NE2 A:HIS431 2.1 15.5 1.0
NE2 A:HIS433 2.1 17.1 1.0
O A:HOH2271 2.5 51.6 1.0
O A:HOH2269 2.5 27.7 1.0
CD2 A:HIS431 3.0 15.2 1.0
CE1 A:HIS592 3.0 19.2 1.0
CD2 A:HIS433 3.0 20.7 1.0
CG A:HIS592 3.1 18.1 1.0
HD2 A:HIS431 3.1 14.9 1.0
CE1 A:HIS433 3.1 19.4 1.0
CE1 A:HIS431 3.1 18.1 1.0
HB3 A:HIS592 3.2 15.9 1.0
HD2 A:HIS433 3.2 18.5 1.0
HE1 A:HIS592 3.2 19.4 1.0
HB2 A:HIS592 3.2 15.9 1.0
HE1 A:HIS433 3.3 18.2 1.0
HE1 A:HIS431 3.3 16.0 1.0
CB A:HIS592 3.4 17.4 1.0
HE2 A:MET602 4.0 17.8 0.5
CG A:HIS431 4.1 13.7 1.0
NE2 A:HIS592 4.1 19.9 1.0
ND1 A:HIS431 4.2 11.8 1.0
ND1 A:HIS433 4.2 16.5 1.0
CG A:HIS433 4.2 14.9 1.0
CD2 A:HIS592 4.2 17.9 1.0
O A:HOH2188 4.4 26.0 1.0
HE2 A:MET602 4.7 19.8 0.5
HE3 A:MET602 4.7 19.8 0.5
O A:HOH2252 4.7 32.7 1.0
H3 A:TPQ382 4.7 29.2 1.0
HG3 A:PRO594 4.7 15.9 1.0
CE A:MET602 4.8 12.7 0.5
SD A:MET602 4.8 29.5 0.5
HG11 A:VAL406 4.8 23.1 1.0
SD A:MET602 4.9 17.6 0.5
CA A:HIS592 4.9 14.4 1.0
O2 A:TPQ382 4.9 27.0 1.0
CE A:MET602 5.0 20.7 0.5

Reference:

D.B.Langley, D.E.Brown, L.E.Cheruzel, S.M.Contakes, A.P.Duff, K.M.Hilmer, D.M.Dooley, H.B.Gray, J.M.Guss, H.C.Freeman. Enantiomer-Specific Binding of Ruthenium(II) Molecular Wires By the Amine Oxidase of Arthrobacter Globiformis. J. Am. Chem. Soc. V. 130 8069 2008.
ISSN: ESSN 1520-5126
PubMed: 18507382
DOI: 10.1021/JA801289F
Page generated: Thu Sep 3 16:33:37 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy