Sodium in PDB 1w6c: Agao Holoenzyme in A Small Cell, at 2.2 Angstroms

All present enzymatic activity of Agao Holoenzyme in A Small Cell, at 2.2 Angstroms:
1.4.3.6;

The structure of Agao Holoenzyme in A Small Cell, at 2.2 Angstroms, PDB code: 1w6c was solved by A.P.Duff, 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)	32.16 / 2.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	158.041, 64.061, 69.693, 90.00, 111.74, 90.00
R / Rfree (%)	17.2 / 21.9

The structure of Agao Holoenzyme in A Small Cell, at 2.2 Angstroms also contains other interesting chemical elements:

Copper

(Cu)

2 atoms

The binding sites of Sodium atom in the Agao Holoenzyme in A Small Cell, at 2.2 Angstroms (pdb code 1w6c). 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 Holoenzyme in A Small Cell, at 2.2 Angstroms, PDB code: 1w6c:

Sodium binding site 1 out of 1 in the Agao Holoenzyme in A Small Cell, at 2.2 Angstroms


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Agao Holoenzyme in A Small Cell, at 2.2 Angstroms within 5.0Å range: probe atom residue distance (Å) B Occ A:Na703 b:29.2 occ:1.00 O A:ILE582 2.4 14.3 1.0 OD1 A:ASP440 2.4 9.3 1.0 O A:MET441 2.4 16.0 1.0 OD1 A:ASP581 2.5 19.3 1.0 O A:HOH2085 2.7 27.1 1.0 H A:ILE582 3.0 16.6 1.0 H A:MET441 3.2 16.1 1.0 N A:ILE582 3.3 17.3 1.0 HH21 A:ARG49 3.3 30.2 1.0 N A:MET441 3.4 15.5 1.0 C A:ILE582 3.4 17.5 1.0 HD1 A:PHE446 3.4 27.6 1.0 C A:MET441 3.4 17.2 1.0 HA A:ASP581 3.6 15.3 1.0 CG A:ASP440 3.7 18.0 1.0 CG A:ASP581 3.8 20.4 1.0 HH22 A:ARG49 3.8 30.2 1.0 C A:ASP440 3.8 16.1 1.0 NH2 A:ARG49 3.9 32.6 1.0 HA A:ASP440 3.9 15.4 1.0 C A:ASP581 3.9 16.2 1.0 HB2 A:MET441 3.9 17.1 1.0 CA A:MET441 3.9 17.4 1.0 CA A:ILE582 3.9 15.7 1.0 HG21 A:VAL583 3.9 15.6 1.0 HB2 A:TYR546 4.0 17.7 1.0 CA A:ASP581 4.2 14.2 1.0 CD1 A:PHE446 4.3 28.1 1.0 CA A:ASP440 4.3 14.8 1.0 HG13 A:ILE582 4.3 18.5 1.0 HE1 A:PHE446 4.4 27.7 1.0 O A:ASP440 4.4 15.6 1.0 OD2 A:ASP440 4.4 23.6 1.0 CB A:MET441 4.4 17.0 1.0 HB2 A:ALA442 4.5 18.2 1.0 HA A:PHE446 4.5 23.2 1.0 HA A:ILE582 4.5 16.6 1.0 HA A:VAL583 4.6 15.3 1.0 HA A:ALA442 4.6 18.7 1.0 N A:VAL583 4.6 15.7 1.0 CB A:ASP581 4.6 16.7 1.0 CB A:ASP440 4.6 14.6 1.0 OD2 A:ASP581 4.6 18.7 1.0 HG12 A:ILE582 4.6 18.5 1.0 N A:ALA442 4.6 20.3 1.0 O A:ASP581 4.7 16.6 1.0 HB3 A:ASN273 4.7 17.5 1.0 HA A:MET441 4.8 16.9 1.0 CE1 A:PHE446 4.8 26.4 1.0 CG2 A:VAL583 4.8 15.0 1.0 CB A:TYR546 4.8 19.1 1.0 CG1 A:ILE582 4.8 19.0 1.0 HG22 A:VAL583 4.8 15.6 1.0 O A:PHE446 4.9 24.9 1.0 HB3 A:TYR546 4.9 17.7 1.0 HB3 A:PHE446 5.0 24.2 1.0

D.B.Langley, A.P.Duff, H.C.Freeman, J.M.Guss. The Copper Containing Amine Oxidase From Arthrobacter Globiformis: Refinement at 1.55 and 2.20 A Resolution in Two Crystal Forms. Acta Crystallogr.,Sect.F V. 62 1052 2006.
ISSN: ESSN 1744-3091
PubMed: 17077478
DOI: 10.1107/S1744309106038814