Atomistry » Copper » PDB 5z86-5zpo » 5zpk
Atomistry »
  Copper »
    PDB 5z86-5zpo »
      5zpk »

Copper in PDB 5zpk: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 at 288 K (2)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 at 288 K (2)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 at 288 K (2):
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 at 288 K (2), PDB code: 5zpk was solved by T.Murakawa, S.Baba, Y.Kawano, H.Hayashi, T.Yano, K.Tanizawa, T.Kumasaka, M.Yamamoto, T.Okajima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.63 / 1.65
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 192.731, 63.767, 158.779, 90.00, 116.85, 90.00
R / Rfree (%) 19.5 / 21.5

Other elements in 5zpk:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 at 288 K (2) also contains other interesting chemical elements:

Sodium (Na) 3 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 at 288 K (2) (pdb code 5zpk). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 at 288 K (2), PDB code: 5zpk:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zpk

Go back to Copper Binding Sites List in 5zpk
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 at 288 K (2)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:11.5
occ:1.00
NE2 A:HIS431 2.0 13.5 1.0
ND1 A:HIS592 2.1 16.6 1.0
NE2 A:HIS433 2.1 12.7 1.0
O A:HOH1003 2.1 21.0 1.0
O A:HOH1185 2.6 8.3 1.0
CE1 A:HIS431 2.9 13.9 1.0
CD2 A:HIS431 3.0 13.6 1.0
CE1 A:HIS592 3.0 16.1 1.0
CD2 A:HIS433 3.0 12.4 1.0
CG A:HIS592 3.1 16.0 1.0
CE1 A:HIS433 3.1 15.8 1.0
CB A:HIS592 3.4 16.1 1.0
O A:HOH1227 3.8 49.4 1.0
ND1 A:HIS431 4.1 14.2 1.0
CG A:HIS431 4.1 14.1 1.0
NE2 A:HIS592 4.1 15.8 1.0
ND1 A:HIS433 4.2 12.6 1.0
CG A:HIS433 4.2 12.4 1.0
CD2 A:HIS592 4.2 15.9 1.0
O A:HOH983 4.4 6.6 1.0
O A:HOH985 4.4 24.8 1.0
SD A:MET602 4.8 24.4 0.5
OX1 A:2TY382 4.8 13.8 1.0
CA A:HIS592 4.9 16.2 1.0
SD A:MET602 5.0 19.7 0.5

Copper binding site 2 out of 2 in 5zpk

Go back to Copper Binding Sites List in 5zpk
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 at 288 K (2)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 6 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:12.4
occ:1.00
NE2 B:HIS431 2.0 12.6 1.0
ND1 B:HIS592 2.0 11.2 1.0
NE2 B:HIS433 2.0 12.7 1.0
O B:HOH991 2.1 19.6 1.0
O B:HOH1196 2.6 12.1 1.0
CE1 B:HIS431 2.9 13.5 1.0
CE1 B:HIS592 3.0 11.9 1.0
CD2 B:HIS431 3.0 10.8 1.0
CE1 B:HIS433 3.0 12.3 1.0
CD2 B:HIS433 3.0 12.0 1.0
CG B:HIS592 3.1 9.3 1.0
CB B:HIS592 3.4 7.7 1.0
O B:HOH1237 4.0 42.1 1.0
ND1 B:HIS431 4.1 12.4 1.0
NE2 B:HIS592 4.1 12.2 1.0
CG B:HIS431 4.1 11.3 1.0
ND1 B:HIS433 4.1 12.6 1.0
CD2 B:HIS592 4.2 11.0 1.0
CG B:HIS433 4.2 11.1 1.0
O B:HOH1109 4.3 22.4 1.0
O B:HOH866 4.4 19.3 1.0
OX1 B:2TY382 4.8 17.0 1.0
SD B:MET602 4.8 16.4 0.4
CE B:MET602 4.9 15.7 0.6
SD B:MET602 4.9 14.8 0.6
CA B:HIS592 4.9 10.2 1.0

Reference:

T.Murakawa, S.Baba, Y.Kawano, H.Hayashi, T.Yano, T.Kumasaka, M.Yamamoto, K.Tanizawa, T.Okajima. In Crystallothermodynamic Analysis of Conformational Change of the Topaquinone Cofactor in Bacterial Copper Amine Oxidase Proc. Natl. Acad. Sci. V. 116 135 2019U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30563857
DOI: 10.1073/PNAS.1811837116
Page generated: Mon Jul 14 05:51:11 2025

Last articles

I in 2BXL
I in 2BMK
I in 2BSQ
I in 2AXE
I in 2BE2
I in 2B5J
I in 1W2Z
I in 2AK4
I in 2ARL
I in 2ANX
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy