Atomistry » Copper » PDB 2cj3-2foy » 2e2t
Atomistry »
  Copper »
    PDB 2cj3-2foy »
      2e2t »

Copper in PDB 2e2t: Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Phenylhydrazine

Enzymatic activity of Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Phenylhydrazine

All present enzymatic activity of Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Phenylhydrazine:
1.4.3.6;

Protein crystallography data

The structure of Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Phenylhydrazine, PDB code: 2e2t was solved by T.Murakawa, T.Okajima, M.Taki, Y.Yamamoto, S.Kuroda, H.Hayashi, K.Tanizawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.50 / 2.05
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.644, 63.081, 91.862, 90.00, 112.16, 90.00
R / Rfree (%) 20.5 / 24.3

Copper Binding Sites:

The binding sites of Copper atom in the Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Phenylhydrazine (pdb code 2e2t). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Phenylhydrazine, PDB code: 2e2t:

Copper binding site 1 out of 1 in 2e2t

Go back to Copper Binding Sites List in 2e2t
Copper binding site 1 out of 1 in the Substrate Schiff-Base Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Phenylhydrazine


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 Analogue of Copper Amine Oxidase From Arthrobacter Globiformis Formed with Phenylhydrazine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1001

b:40.3
occ:1.00
 NE2 A:HIS433 2.1 35.8 1.0
NE2 A:HIS431 2.2 40.0 1.0
ND1 A:HIS592 2.3 41.1 1.0
O A:HOH1352 2.4 42.9 1.0
O A:HOH1188 2.7 55.2 1.0
CD2 A:HIS433 2.9 33.3 1.0
CD2 A:HIS431 3.1 36.6 1.0
CG A:HIS592 3.2 40.0 1.0
CE1 A:HIS431 3.2 37.5 1.0
CE1 A:HIS433 3.2 36.9 1.0
CE1 A:HIS592 3.3 40.7 1.0
CB A:HIS592 3.4 37.1 1.0
CG A:HIS433 4.2 34.3 1.0
CG A:HIS431 4.2 35.9 1.0
ND1 A:HIS433 4.2 36.1 1.0
ND1 A:HIS431 4.3 36.9 1.0
CD2 A:HIS592 4.4 40.0 1.0
NE2 A:HIS592 4.4 40.2 1.0
O A:HOH1180 4.4 46.2 1.0
OX1 A:YPZ382 4.4 54.0 1.0
O A:HOH1400 4.5 54.2 1.0
CE A:MET602 4.9 45.9 1.0
SD A:MET602 4.9 52.0 1.0
CA A:HIS592 4.9 36.5 1.0

Reference:

T.Murakawa, T.Okajima, M.Taki, Y.Yamamoto, S.Kuroda, H.Hayashi, K.Tanizawa. Catalytic Regulation Conducted By the Substrate Schiff Base and Conserved Aspartic Acid Residue in Bacterial Copper Amine Oxidase Reaction To Be Published.
Page generated: Mon Jul 14 00:54:58 2025

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy