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Copper in PDB 2cfw: Agao in Complex with WC7A (Ru-Wire Inhibitor, 7-Carbon Linker, Data Set A)

Enzymatic activity of Agao in Complex with WC7A (Ru-Wire Inhibitor, 7-Carbon Linker, Data Set A)

All present enzymatic activity of Agao in Complex with WC7A (Ru-Wire Inhibitor, 7-Carbon Linker, Data Set A):
1.4.3.6;

Protein crystallography data

The structure of Agao in Complex with WC7A (Ru-Wire Inhibitor, 7-Carbon Linker, Data Set A), PDB code: 2cfw 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) 25.85 / 1.74
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 158.049, 62.744, 92.064, 90.00, 112.10, 90.00
R / Rfree (%) 16.1 / 17.6

Other elements in 2cfw:

The structure of Agao in Complex with WC7A (Ru-Wire Inhibitor, 7-Carbon Linker, Data Set A) also contains other interesting chemical elements:

Ruthenium (Ru) 1 atom
Sodium (Na) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Agao in Complex with WC7A (Ru-Wire Inhibitor, 7-Carbon Linker, Data Set A) (pdb code 2cfw). 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 WC7A (Ru-Wire Inhibitor, 7-Carbon Linker, Data Set A), PDB code: 2cfw:

Copper binding site 1 out of 1 in 2cfw

Go back to Copper Binding Sites List in 2cfw
Copper binding site 1 out of 1 in the Agao in Complex with WC7A (Ru-Wire Inhibitor, 7-Carbon Linker, Data Set A)


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 WC7A (Ru-Wire Inhibitor, 7-Carbon Linker, Data Set A) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:24.6
occ:1.00
 NE2 A:HIS431 2.1 15.9 1.0
NE2 A:HIS433 2.1 15.7 1.0
ND1 A:HIS592 2.1 20.0 1.0
O A:HOH2234 2.1 47.6 1.0
O A:HOH2205 2.8 24.7 1.0
CD2 A:HIS431 3.0 15.5 1.0
CD2 A:HIS433 3.0 16.8 1.0
CE1 A:HIS592 3.1 19.4 1.0
CG A:HIS592 3.1 18.1 1.0
CE1 A:HIS433 3.1 16.2 1.0
CE1 A:HIS431 3.1 16.3 1.0
HD2 A:HIS431 3.1 15.3 1.0
HB2 A:HIS592 3.2 16.0 1.0
HB3 A:HIS592 3.2 16.0 1.0
HD2 A:HIS433 3.2 15.9 1.0
HE1 A:HIS592 3.2 19.3 1.0
HE1 A:HIS433 3.3 15.6 1.0
HE1 A:HIS431 3.3 15.6 1.0
CB A:HIS592 3.3 16.3 1.0
HE3 A:MET602 4.0 20.9 0.3
CG A:HIS431 4.1 14.4 1.0
ND1 A:HIS431 4.1 13.5 1.0
ND1 A:HIS433 4.2 14.0 1.0
NE2 A:HIS592 4.2 18.6 1.0
CG A:HIS433 4.2 14.0 1.0
CD2 A:HIS592 4.2 19.0 1.0
HE2 A:MET602 4.4 15.6 0.3
O A:HOH2158 4.5 21.4 1.0
O A:HOH2217 4.6 28.0 1.0
HG11 A:VAL406 4.7 19.9 1.0
CE A:MET602 4.7 22.3 0.3
H3 A:TPQ382 4.8 28.5 1.0
HG3 A:PRO594 4.8 16.0 1.0
CE A:MET602 4.8 21.5 0.3
CA A:HIS592 4.9 15.4 1.0
SD A:MET602 4.9 16.2 0.3
SD A:MET602 4.9 23.1 0.3
O2 A:TPQ382 4.9 24.0 1.0
SD A:MET602 5.0 19.6 0.3

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: ISSN 0002-7863
PubMed: 18507382
DOI: 10.1021/JA801289F
Page generated: Mon Jul 14 00:52:12 2025

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