Atomistry » Copper » PDB 1rju-1tl4 » 1spu
Atomistry »
  Copper »
    PDB 1rju-1tl4 »
      1spu »

Copper in PDB 1spu: Structure of Oxidoreductase

Enzymatic activity of Structure of Oxidoreductase

All present enzymatic activity of Structure of Oxidoreductase:
1.4.3.6;

Protein crystallography data

The structure of Structure of Oxidoreductase, PDB code: 1spu was solved by C.M.Wilmot, S.E.V.Phillips, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 134.460, 166.070, 79.410, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / n/a

Other elements in 1spu:

The structure of Structure of Oxidoreductase also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Copper Binding Sites:

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

Copper binding site 1 out of 2 in 1spu

Go back to Copper Binding Sites List in 1spu
Copper binding site 1 out of 2 in the Structure of Oxidoreductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Oxidoreductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu800

b:25.2
occ:1.00
NE2 A:HIS526 2.1 17.7 1.0
ND1 A:HIS689 2.3 13.6 1.0
NE2 A:HIS524 2.4 27.8 1.0
O A:HOH1277 2.4 22.9 1.0
O A:HOH1422 2.9 52.2 1.0
CD2 A:HIS526 2.9 21.0 1.0
CD2 A:HIS524 3.1 17.1 1.0
CG A:HIS689 3.2 19.4 1.0
CE1 A:HIS526 3.2 18.4 1.0
CE1 A:HIS524 3.3 20.8 1.0
CE1 A:HIS689 3.3 23.8 1.0
CB A:HIS689 3.3 14.6 1.0
O A:HOH1057 4.1 24.4 1.0
CG A:HIS526 4.1 15.1 1.0
CG A:HIS524 4.2 24.0 1.0
ND1 A:HIS526 4.3 18.8 1.0
ND1 A:HIS524 4.3 19.1 1.0
CD2 A:HIS689 4.3 22.0 1.0
NE2 A:HIS689 4.4 22.2 1.0
SD A:MET699 4.6 58.5 1.0
O A:HOH1292 4.6 21.3 1.0
O2 A:PAQ466 4.7 20.3 1.0
CA A:HIS689 4.9 10.7 1.0

Copper binding site 2 out of 2 in 1spu

Go back to Copper Binding Sites List in 1spu
Copper binding site 2 out of 2 in the Structure of Oxidoreductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of Oxidoreductase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu800

b:20.9
occ:1.00
NE2 B:HIS526 2.0 17.3 1.0
ND1 B:HIS689 2.3 13.3 1.0
NE2 B:HIS524 2.4 19.4 1.0
O B:HOH1443 2.7 16.1 1.0
O B:HOH1518 3.0 49.2 1.0
CD2 B:HIS526 3.0 14.9 1.0
CE1 B:HIS526 3.1 14.0 1.0
CD2 B:HIS524 3.1 8.0 1.0
CG B:HIS689 3.2 14.6 1.0
CE1 B:HIS689 3.4 15.0 1.0
CB B:HIS689 3.4 12.0 1.0
CE1 B:HIS524 3.5 13.8 1.0
ND1 B:HIS526 4.2 18.7 1.0
CG B:HIS526 4.2 11.5 1.0
O B:HOH1283 4.3 35.9 1.0
CG B:HIS524 4.3 13.7 1.0
CD2 B:HIS689 4.4 6.9 1.0
NE2 B:HIS689 4.4 18.7 1.0
ND1 B:HIS524 4.4 19.6 1.0
O B:HOH1214 4.6 14.5 1.0
CE B:MET699 4.7 21.6 1.0
O2 B:PAQ466 4.7 22.6 1.0
SD B:MET699 4.7 34.3 1.0
O B:HOH1508 4.7 28.1 1.0
CE1 B:HIS613 4.8 15.8 1.0
CA B:HIS689 4.9 16.2 1.0
O B:HOH1442 5.0 22.1 1.0

Reference:

C.M.Wilmot, J.M.Murray, G.Alton, M.R.Parsons, M.A.Convery, V.Blakeley, A.S.Corner, M.M.Palcic, P.F.Knowles, M.J.Mcpherson, S.E.Phillips. Catalytic Mechanism of the Quinoenzyme Amine Oxidase From Escherichia Coli: Exploring the Reductive Half-Reaction. Biochemistry V. 36 1608 1997.
ISSN: ISSN 0006-2960
PubMed: 9048544
DOI: 10.1021/BI962205J
Page generated: Tue Jul 30 22:47:32 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy