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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

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: Thu Sep 3 16:19:38 2020
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