Sodium in PDB 1w5z: Agao Covalent Complex with Benzylhydrazine

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

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

The structure of Agao Covalent Complex with Benzylhydrazine also contains other interesting chemical elements:

Copper

(Cu)

1 atom

The binding sites of Sodium atom in the Agao Covalent Complex with Benzylhydrazine (pdb code 1w5z). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Agao Covalent Complex with Benzylhydrazine, PDB code: 1w5z:

Sodium binding site 1 out of 1 in the Agao Covalent Complex with Benzylhydrazine


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Agao Covalent Complex with Benzylhydrazine within 5.0Å range: probe atom residue distance (Å) B Occ A:Na703 b:30.6 occ:1.00 OD1 A:ASP440 2.3 11.7 1.0 OD1 A:ASP581 2.4 12.5 1.0 O A:MET441 2.4 12.2 1.0 O A:ILE582 2.4 8.7 1.0 O A:HOH2340 2.8 28.7 1.0 H A:ILE582 2.9 8.6 1.0 HD1 A:PHE446 3.1 20.2 1.0 H A:MET441 3.2 9.8 1.0 N A:ILE582 3.3 9.0 1.0 N A:MET441 3.4 10.0 1.0 C A:ILE582 3.4 8.2 1.0 C A:MET441 3.4 7.8 1.0 HH21 A:ARG49 3.5 16.6 1.0 CG A:ASP440 3.6 14.8 1.0 HA A:ASP581 3.6 10.2 1.0 CG A:ASP581 3.6 17.7 1.0 C A:ASP440 3.8 10.3 1.0 HB2 A:MET441 3.8 8.4 1.0 C A:ASP581 3.9 8.9 1.0 CA A:MET441 3.9 9.1 1.0 HA A:ASP440 3.9 9.1 1.0 CA A:ILE582 3.9 7.4 1.0 CD1 A:PHE446 3.9 23.4 1.0 HE1 A:PHE446 4.0 21.4 1.0 HB2 A:TYR546 4.0 10.6 1.0 HG21 A:VAL583 4.1 11.8 1.0 CA A:ASP581 4.1 9.8 1.0 NH2 A:ARG49 4.1 13.7 1.0 HH22 A:ARG49 4.1 16.6 1.0 CA A:ASP440 4.2 8.4 1.0 OD2 A:ASP440 4.3 11.9 1.0 HG12 A:ILE582 4.4 12.6 1.0 CB A:MET441 4.4 6.8 1.0 CE1 A:PHE446 4.4 19.0 1.0 O A:ASP440 4.4 7.8 1.0 OD2 A:ASP581 4.5 16.0 1.0 CB A:ASP581 4.5 13.6 1.0 HA A:ILE582 4.5 8.1 1.0 HA A:PHE446 4.5 12.9 1.0 CB A:ASP440 4.5 12.0 1.0 N A:VAL583 4.5 11.8 1.0 HA A:VAL583 4.6 10.9 1.0 HA A:ALA442 4.6 8.0 1.0 N A:ALA442 4.6 8.1 1.0 HG22 A:VAL583 4.7 11.8 1.0 HB3 A:ASN273 4.7 10.7 1.0 HB2 A:ALA442 4.7 9.0 1.0 HG13 A:ILE582 4.7 12.6 1.0 O A:ASP581 4.7 10.1 1.0 HA A:MET441 4.8 8.6 1.0 CG2 A:VAL583 4.8 12.3 1.0 HB3 A:PHE446 4.9 13.4 1.0 CG1 A:ILE582 4.9 14.2 1.0 CB A:TYR546 4.9 9.2 1.0 O A:PHE446 4.9 10.7 1.0 HB3 A:TYR546 5.0 10.6 1.0 HB3 A:MET441 5.0 8.4 1.0

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