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Copper in PDB 1jrq: X-Ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. Coli Amine Oxidase

Enzymatic activity of X-Ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. Coli Amine Oxidase

All present enzymatic activity of X-Ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. Coli Amine Oxidase:
1.4.3.4;

Protein crystallography data

The structure of X-Ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. Coli Amine Oxidase, PDB code: 1jrq was solved by J.M.Murray, C.R.Kurtis, W.Tambarajah, C.G.Saysell, C.M.Wilmot, M.R.Parsons, S.E.V.Phillips, P.F.Knowles, M.J.Mcpherson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 134.540, 166.450, 79.380, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 23.5

Copper Binding Sites:

The binding sites of Copper atom in the X-Ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. Coli Amine Oxidase (pdb code 1jrq). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the X-Ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. Coli Amine Oxidase, PDB code: 1jrq:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1jrq

Go back to Copper Binding Sites List in 1jrq
Copper binding site 1 out of 2 in the X-Ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. Coli Amine Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of X-Ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. Coli Amine Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu801

b:28.2
occ:1.00
 NE2 A:HIS526 2.2 20.2 1.0
ND1 A:HIS689 2.3 24.6 1.0
NE2 A:HIS524 2.3 26.2 1.0
O A:HOH1216 2.7 38.5 1.0
CD2 A:HIS526 2.8 20.7 1.0
CE1 A:HIS689 3.1 24.0 1.0
CD2 A:HIS524 3.1 24.7 1.0
CG A:HIS689 3.2 24.2 1.0
CE1 A:HIS524 3.2 25.0 1.0
CE1 A:HIS526 3.3 22.9 1.0
CB A:HIS689 3.4 26.1 1.0
O A:HOH964 3.7 40.2 1.0
O A:HOH1255 3.7 46.8 1.0
CG A:HIS526 4.1 21.9 1.0
NE2 A:HIS689 4.2 26.0 1.0
ND1 A:HIS526 4.2 23.4 1.0
CG A:HIS524 4.3 26.2 1.0
CD2 A:HIS689 4.3 24.3 1.0
ND1 A:HIS524 4.3 26.7 1.0
O A:HOH1522 4.4 39.9 1.0
CE1 A:HIS613 4.7 22.9 1.0
SD A:MET699 4.8 39.1 1.0
O4 A:TPQ466 4.9 43.0 1.0
CA A:HIS689 5.0 25.0 1.0

Copper binding site 2 out of 2 in 1jrq

Go back to Copper Binding Sites List in 1jrq
Copper binding site 2 out of 2 in the X-Ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. Coli Amine Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of X-Ray Structure Analysis of the Role of the Conserved Tyrosine-369 in Active Site of E. Coli Amine Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu801

b:28.4
occ:1.00
 NE2 B:HIS526 2.3 21.7 1.0
NE2 B:HIS524 2.3 25.0 1.0
ND1 B:HIS689 2.3 21.7 1.0
O B:HOH1201 2.4 24.0 1.0
O B:HOH1017 2.7 41.0 1.0
CD2 B:HIS526 3.0 18.9 1.0
CD2 B:HIS524 3.2 24.0 1.0
CG B:HIS689 3.2 22.2 1.0
CE1 B:HIS524 3.2 24.6 1.0
CE1 B:HIS689 3.3 21.2 1.0
CB B:HIS689 3.4 22.8 1.0
CE1 B:HIS526 3.4 22.8 1.0
O B:HOH1154 3.6 37.7 1.0
O B:HOH997 4.2 32.6 1.0
CG B:HIS526 4.2 19.9 1.0
CG B:HIS524 4.3 24.9 1.0
O5 B:TPQ466 4.3 49.9 1.0
ND1 B:HIS524 4.3 25.3 1.0
ND1 B:HIS526 4.4 23.4 1.0
CD2 B:HIS689 4.4 20.3 1.0
NE2 B:HIS689 4.4 22.2 1.0
O4 B:TPQ466 4.6 46.2 1.0
C5 B:TPQ466 4.6 50.9 1.0
O B:HOH818 4.7 37.5 1.0
SD B:MET699 4.7 44.2 1.0
C4 B:TPQ466 4.8 48.3 1.0
O B:HOH1324 4.9 40.3 1.0
NE2 B:HIS613 4.9 23.1 1.0
CA B:HIS689 4.9 23.9 1.0

Reference:

J.M.Murray, C.R.Kurtis, W.Tambyrajah, C.G.Saysell, C.M.Wilmot, M.R.Parsons, S.E.Phillips, P.F.Knowles, M.J.Mcpherson. Conserved Tyrosine-369 in the Active Site of Escherichia Coli Copper Amine Oxidase Is Not Essential. Biochemistry V. 40 12808 2001.
ISSN: ISSN 0006-2960
PubMed: 11669617
DOI: 10.1021/BI011187P
Page generated: Thu Sep 3 16:02:08 2020
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