Copper in PDB 2d1w: Substrate Schiff-Base Intermediate with Tyramine in Copper Amine Oxidase From Arthrobacter Globiformis

All present enzymatic activity of Substrate Schiff-Base Intermediate with Tyramine in Copper Amine Oxidase From Arthrobacter Globiformis:
1.4.3.6;

The structure of Substrate Schiff-Base Intermediate with Tyramine in Copper Amine Oxidase From Arthrobacter Globiformis, PDB code: 2d1w was solved by T.Murakawa, T.Okajima, S.Kuroda, T.Nakamoto, M.Taki, Y.Yamamoto, H.Hayashi, K.Tanizawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.44 / 1.74
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	157.570, 63.351, 183.651, 90.00, 112.29, 90.00
R / Rfree (%)	19 / 21.7

The binding sites of Copper atom in the Substrate Schiff-Base Intermediate with Tyramine in Copper Amine Oxidase From Arthrobacter Globiformis (pdb code 2d1w). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Substrate Schiff-Base Intermediate with Tyramine in Copper Amine Oxidase From Arthrobacter Globiformis, PDB code: 2d1w:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Substrate Schiff-Base Intermediate with Tyramine in Copper Amine Oxidase From Arthrobacter Globiformis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Substrate Schiff-Base Intermediate with Tyramine in Copper Amine Oxidase From Arthrobacter Globiformis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1001 b:27.3 occ:1.00 NE2 A:HIS431 2.1 22.2 1.0 NE2 A:HIS433 2.1 24.8 1.0 ND1 A:HIS592 2.2 28.7 1.0 O A:HOH1361 2.3 45.1 1.0 O A:HOH1125 2.5 36.6 1.0 CD2 A:HIS433 3.0 25.2 1.0 CE1 A:HIS431 3.0 22.7 1.0 CD2 A:HIS431 3.0 21.4 1.0 CG A:HIS592 3.2 27.1 1.0 CE1 A:HIS433 3.2 26.4 1.0 CE1 A:HIS592 3.3 28.3 1.0 CB A:HIS592 3.3 24.9 1.0 O A:HOH1298 3.7 49.1 1.0 ND1 A:HIS431 4.1 21.6 1.0 CG A:HIS433 4.2 24.5 1.0 CG A:HIS431 4.2 21.4 1.0 ND1 A:HIS433 4.2 23.7 1.0 O A:HOH1081 4.3 27.9 1.0 CD2 A:HIS592 4.3 27.3 1.0 NE2 A:HIS592 4.4 28.1 1.0 OD1 A:TTS382 4.5 42.8 0.5 O A:HOH1127 4.5 37.6 1.0 OD1 A:TTS382 4.6 42.7 0.5 CA A:HIS592 4.9 22.1 1.0 SD A:MET602 4.9 37.6 1.0

Copper binding site 2 out of 2 in the Substrate Schiff-Base Intermediate with Tyramine in Copper Amine Oxidase From Arthrobacter Globiformis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Substrate Schiff-Base Intermediate with Tyramine in Copper Amine Oxidase From Arthrobacter Globiformis within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu1002 b:27.6 occ:1.00 NE2 B:HIS431 2.1 22.4 1.0 NE2 B:HIS433 2.1 23.3 1.0 ND1 B:HIS592 2.2 29.9 1.0 O B:HOH1285 2.5 37.7 1.0 CD2 B:HIS433 2.9 25.6 1.0 CE1 B:HIS431 3.1 23.0 1.0 CD2 B:HIS431 3.1 23.8 1.0 CG B:HIS592 3.1 29.0 1.0 CE1 B:HIS592 3.2 30.0 1.0 CE1 B:HIS433 3.3 25.5 1.0 CB B:HIS592 3.4 25.3 1.0 O B:HOH1547 3.6 56.2 1.0 CG B:HIS433 4.1 22.7 1.0 ND1 B:HIS431 4.2 22.1 1.0 CG B:HIS431 4.2 22.9 1.0 O B:HOH1296 4.2 45.2 1.0 ND1 B:HIS433 4.3 22.9 1.0 CD2 B:HIS592 4.3 29.9 1.0 NE2 B:HIS592 4.3 29.4 1.0 O B:HOH1154 4.4 27.3 1.0 OD1 B:TTS382 4.5 43.5 0.5 OD1 B:TTS382 4.6 42.1 0.5 SD B:MET602 4.8 39.7 1.0 CA B:HIS592 4.9 23.7 1.0

T.Murakawa, T.Okajima, S.Kuroda, T.Nakamoto, M.Taki, Y.Yamamoto, H.Hayashi, K.Tanizawa. Quantum Mechanical Hydrogen Tunneling in Bacterial Copper Amine Oxidase Reaction Biochem.Biophys.Res.Commun. V. 342 414 2006.
ISSN: ISSN 0006-291X
PubMed: 16487484
DOI: 10.1016/J.BBRC.2006.01.150