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Copper in PDB 1w5z: Agao Covalent Complex with Benzylhydrazine

Enzymatic activity of Agao Covalent Complex with Benzylhydrazine

All present enzymatic activity of Agao Covalent Complex with Benzylhydrazine:
1.4.3.6;

Protein crystallography data

The structure of Agao Covalent Complex with Benzylhydrazine, PDB code: 1w5z was solved by A.P.Duff, D.M.Trambaiolo, D.B.Langley, G.A.Juda, E.M.Shepard, D.M.Dooley, H.C.Freeman, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.85 / 1.86
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 158.126, 62.665, 92.283, 90.00, 112.07, 90.00
R / Rfree (%) 15.2 / 18.7

Copper Binding Sites:

The binding sites of Copper atom in the Agao Covalent Complex with Benzylhydrazine (pdb code 1w5z). 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 Covalent Complex with Benzylhydrazine, PDB code: 1w5z:

Copper binding site 1 out of 1 in 1w5z

Go back to Copper Binding Sites List in 1w5z
Copper binding site 1 out of 1 in the Agao Covalent Complex with Benzylhydrazine


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Agao Covalent Complex with Benzylhydrazine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:31.2
occ:1.00
NE2 A:HIS433 2.0 7.7 1.0
ND1 A:HIS592 2.1 17.3 1.0
NE2 A:HIS431 2.1 11.8 1.0
O A:HOH2468 2.2 54.1 1.0
O A:HOH2301 2.6 35.2 1.0
CD2 A:HIS431 3.0 8.5 1.0
CD2 A:HIS433 3.0 12.9 1.0
CE1 A:HIS592 3.1 16.3 1.0
CE1 A:HIS433 3.1 10.8 1.0
CG A:HIS592 3.1 16.5 1.0
HD2 A:HIS431 3.1 9.4 1.0
CE1 A:HIS431 3.1 11.5 1.0
HD2 A:HIS433 3.1 10.1 1.0
HB3 A:HIS592 3.2 13.8 1.0
HB2 A:HIS592 3.2 13.8 1.0
HE1 A:HIS592 3.2 15.9 1.0
HE1 A:HIS433 3.3 9.7 1.0
HE1 A:HIS431 3.3 11.3 1.0
CB A:HIS592 3.4 15.9 1.0
CG A:HIS431 4.1 9.2 1.0
CG A:HIS433 4.1 6.0 1.0
ND1 A:HIS433 4.1 9.3 1.0
NE2 A:HIS592 4.2 13.6 1.0
ND1 A:HIS431 4.2 10.2 1.0
CD2 A:HIS592 4.2 17.0 1.0
HE3 A:MET602 4.2 29.6 1.0
O A:HOH2234 4.4 26.9 1.0
HG11 A:VAL406 4.7 17.2 1.0
H3 A:3TY382 4.7 19.5 1.0
O A:HOH2317 4.7 39.7 1.0
O2 A:3TY382 4.8 18.6 1.0
HG3 A:PRO594 4.8 10.9 1.0
CA A:HIS592 4.9 12.0 1.0
SD A:MET602 4.9 28.7 1.0
CE A:MET602 4.9 30.0 1.0

Reference:

D.B.Langley, D.M.Trambaiolo, A.P.Duff, D.M.Dooley, H.C.Freeman, J.M.Guss. Complexes of the Copper-Containing Amine Oxidase From Arthrobacter Globiformis with the Inhibitors Benzylhydrazine and Tranylcypromine. Acta Crystallogr.,Sect.F V. 64 577 2008.
ISSN: ESSN 1744-3091
PubMed: 18607080
DOI: 10.1107/S174430910801556X
Page generated: Thu Sep 3 16:23:37 2020
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