Copper in PDB 1w6g: Agao Holoenzyme at 1.55 Angstroms

All present enzymatic activity of Agao Holoenzyme at 1.55 Angstroms:
1.4.3.6;

The structure of Agao Holoenzyme at 1.55 Angstroms, PDB code: 1w6g was solved by D.B.Langley, A.P.Duff, 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)	25.82 / 1.55
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	157.836, 63.243, 91.982, 90.00, 112.03, 90.00
R / Rfree (%)	17 / 18.8

The structure of Agao Holoenzyme at 1.55 Angstroms also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Copper atom in the Agao Holoenzyme at 1.55 Angstroms (pdb code 1w6g). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Agao Holoenzyme at 1.55 Angstroms, PDB code: 1w6g:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Agao Holoenzyme at 1.55 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Agao Holoenzyme at 1.55 Angstroms within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu701 b:30.2 occ:1.00 NE2 A:HIS431 2.0 5.5 1.0 ND1 A:HIS592 2.0 11.0 0.8 NE2 A:HIS433 2.1 10.9 1.0 O4 A:TPQ382 2.2 26.8 0.3 ND1 A:HIS592 2.2 6.0 0.2 O A:HOH2292 2.3 37.2 0.7 O A:HOH2293 2.7 31.4 0.7 CE1 A:HIS592 3.0 7.9 0.8 CD2 A:HIS431 3.0 4.6 1.0 CE1 A:HIS431 3.0 5.0 1.0 CD2 A:HIS433 3.0 9.5 1.0 CE1 A:HIS433 3.1 10.3 1.0 CG A:HIS592 3.1 5.3 0.8 HE1 A:HIS592 3.1 7.9 0.8 CG A:HIS592 3.1 6.2 0.2 HB2 A:HIS592 3.1 6.0 0.2 HD2 A:HIS431 3.2 4.7 1.0 CE1 A:HIS592 3.2 3.5 0.2 C4 A:TPQ382 3.2 19.7 0.3 HD2 A:HIS433 3.2 8.9 1.0 HB3 A:HIS592 3.2 6.3 0.8 HE1 A:HIS431 3.2 4.9 1.0 HB2 A:HIS592 3.2 6.3 0.8 HB3 A:HIS592 3.3 6.0 0.2 HE1 A:HIS433 3.3 10.0 1.0 HE1 A:HIS592 3.4 3.9 0.2 CB A:HIS592 3.4 6.5 0.2 CB A:HIS592 3.4 7.8 0.8 O5 A:TPQ382 3.8 9.3 0.3 C5 A:TPQ382 3.9 19.2 0.3 C3 A:TPQ382 4.1 18.6 0.3 ND1 A:HIS431 4.1 4.1 1.0 NE2 A:HIS592 4.1 4.6 0.8 CG A:HIS431 4.1 4.1 1.0 H3 A:TPQ382 4.2 18.6 0.3 ND1 A:HIS433 4.2 8.5 1.0 CG A:HIS433 4.2 5.6 1.0 CD2 A:HIS592 4.2 6.0 0.8 HE3 A:MET602 4.2 27.0 0.5 NE2 A:HIS592 4.3 2.5 0.2 CD2 A:HIS592 4.3 7.7 0.2 HE3 A:MET602 4.4 20.4 0.5 O A:HOH2217 4.4 31.2 1.0 HG3 A:PRO594 4.7 6.2 1.0 SD A:MET602 4.8 32.9 0.5 SD A:MET602 4.8 29.5 0.5 HG11 A:VAL406 4.9 17.5 1.0 CA A:HIS592 4.9 5.7 1.0 CE A:MET602 5.0 24.4 0.5 CE A:MET602 5.0 16.4 0.5

Copper binding site 2 out of 2 in the Agao Holoenzyme at 1.55 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Agao Holoenzyme at 1.55 Angstroms within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu702 b:35.3 occ:0.40 ND1 A:HIS201 1.9 7.7 0.5 NE2 A:HIS170 2.0 10.9 1.0 OD2 A:ASP165 2.3 15.9 1.0 OD2 A:ASP161 2.3 16.0 1.0 HE1 A:HIS201 2.5 11.0 0.5 CE1 A:HIS201 2.6 14.0 0.5 OD1 A:ASP165 2.8 14.8 1.0 CG A:ASP165 2.9 15.0 1.0 CE1 A:HIS170 3.0 12.8 1.0 CD2 A:HIS170 3.0 12.8 1.0 HB2 A:ASP161 3.0 13.1 1.0 HE1 A:HIS170 3.2 11.5 1.0 HD2 A:HIS170 3.2 11.4 1.0 CG A:HIS201 3.2 12.1 0.5 CG A:ASP161 3.2 15.8 1.0 HB3 A:HIS201 3.4 14.1 0.5 HA A:HIS201 3.5 14.7 1.0 O A:HOH2137 3.5 32.5 1.0 HB2 A:HIS201 3.6 14.1 0.5 CB A:ASP161 3.6 13.0 1.0 H A:ASP161 3.8 12.1 1.0 HB3 A:HIS201 3.8 14.2 0.5 NE2 A:HIS201 3.8 7.6 0.5 CB A:HIS201 3.8 14.5 0.5 CB A:HIS201 3.9 14.4 0.5 ND1 A:HIS170 4.1 8.9 1.0 CG A:HIS170 4.1 8.6 1.0 H31 A:GOL752 4.1 49.7 1.0 CD2 A:HIS201 4.1 13.8 0.5 CA A:HIS201 4.1 14.7 1.0 HE1 A:PHE162 4.2 19.0 1.0 HB3 A:ASP161 4.3 13.1 1.0 OD1 A:ASP161 4.3 21.3 1.0 CB A:ASP165 4.3 10.1 1.0 N A:ASP161 4.4 12.3 1.0 HB2 A:ASP165 4.5 11.5 1.0 HB3 A:ALA169 4.6 8.3 1.0 HB3 A:ASP165 4.7 11.5 1.0 CA A:ASP161 4.7 12.5 1.0 CE1 A:PHE162 4.7 19.0 1.0 N A:HIS201 4.7 14.7 1.0 HB2 A:HIS201 4.8 14.2 0.5 O A:ALA199 4.9 14.2 1.0 H A:GLY202 4.9 14.5 1.0 ND2 A:ASN203 5.0 12.5 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