Sodium in PDB 2wof: Edta Treated E. Coli Copper Amine Oxidase
Enzymatic activity of Edta Treated E. Coli Copper Amine Oxidase
All present enzymatic activity of Edta Treated E. Coli Copper Amine Oxidase:
1.4.3.6;
Protein crystallography data
The structure of Edta Treated E. Coli Copper Amine Oxidase, PDB code: 2wof
was solved by
M.A.Smith,
P.Pirrat,
A.R.Pearson,
P.F.Knowles,
S.E.V.Phillips,
M.J.Mcpherson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.96 /
2.25
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
135.079,
166.880,
79.802,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.686 /
22.041
|
Other elements in 2wof:
The structure of Edta Treated E. Coli Copper Amine Oxidase also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Edta Treated E. Coli Copper Amine Oxidase
(pdb code 2wof). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 4 binding sites of Sodium where determined in the
Edta Treated E. Coli Copper Amine Oxidase, PDB code: 2wof:
Jump to Sodium binding site number:
1;
2;
3;
4;
Sodium binding site 1 out
of 4 in 2wof
Go back to
Sodium Binding Sites List in 2wof
Sodium binding site 1 out
of 4 in the Edta Treated E. Coli Copper Amine Oxidase
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Edta Treated E. Coli Copper Amine Oxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na1727
b:30.9
occ:1.00
|
OE2
|
A:GLU573
|
2.3
|
33.9
|
1.0
|
O
|
A:TYR667
|
2.3
|
30.1
|
1.0
|
O
|
A:HOH2554
|
2.5
|
39.6
|
1.0
|
OE1
|
A:GLU672
|
2.7
|
42.5
|
1.0
|
OE1
|
A:GLU573
|
2.9
|
33.0
|
1.0
|
CD
|
A:GLU573
|
3.0
|
34.9
|
1.0
|
O
|
A:HOH2574
|
3.1
|
43.2
|
1.0
|
C
|
A:TYR667
|
3.5
|
32.9
|
1.0
|
CD
|
A:GLU672
|
3.8
|
43.8
|
1.0
|
OE1
|
A:GLU647
|
4.2
|
29.3
|
1.0
|
CG
|
A:GLU672
|
4.2
|
40.6
|
1.0
|
N
|
A:ARG642
|
4.3
|
30.0
|
1.0
|
CA
|
A:TYR667
|
4.4
|
32.7
|
1.0
|
N
|
A:SER668
|
4.5
|
34.7
|
1.0
|
CG
|
A:GLU573
|
4.5
|
34.5
|
1.0
|
CB
|
A:THR641
|
4.5
|
30.9
|
1.0
|
CA
|
A:SER668
|
4.5
|
36.1
|
1.0
|
OE2
|
A:GLU647
|
4.6
|
33.9
|
1.0
|
CB
|
A:ARG642
|
4.6
|
31.6
|
1.0
|
CB
|
A:TYR667
|
4.8
|
32.6
|
1.0
|
O
|
A:ARG642
|
4.8
|
29.0
|
1.0
|
CG2
|
A:THR641
|
4.8
|
31.5
|
1.0
|
CD
|
A:GLU647
|
4.8
|
32.6
|
1.0
|
OE2
|
A:GLU672
|
4.9
|
47.8
|
1.0
|
CA
|
A:ARG642
|
5.0
|
31.0
|
1.0
|
|
Sodium binding site 2 out
of 4 in 2wof
Go back to
Sodium Binding Sites List in 2wof
Sodium binding site 2 out
of 4 in the Edta Treated E. Coli Copper Amine Oxidase
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Edta Treated E. Coli Copper Amine Oxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na1728
b:26.8
occ:1.00
|
O
|
A:ALA679
|
2.3
|
28.1
|
1.0
|
OD1
|
A:ASP533
|
2.4
|
25.6
|
1.0
|
OD1
|
A:ASP678
|
2.4
|
29.8
|
1.0
|
OD1
|
A:ASP535
|
2.4
|
29.1
|
1.0
|
O
|
A:LEU534
|
2.4
|
25.9
|
1.0
|
O
|
A:HOH2477
|
2.7
|
22.4
|
1.0
|
C
|
A:LEU534
|
3.3
|
26.4
|
1.0
|
C
|
A:ALA679
|
3.4
|
28.2
|
1.0
|
N
|
A:ALA679
|
3.5
|
29.9
|
1.0
|
NZ
|
A:LYS133
|
3.5
|
21.6
|
1.0
|
CG
|
A:ASP533
|
3.6
|
25.3
|
1.0
|
CG
|
A:ASP678
|
3.6
|
31.9
|
1.0
|
CG
|
A:ASP535
|
3.7
|
28.2
|
1.0
|
N
|
A:LEU534
|
3.9
|
26.9
|
1.0
|
C
|
A:ASP533
|
4.0
|
25.9
|
1.0
|
CA
|
A:ALA679
|
4.0
|
29.5
|
1.0
|
N
|
A:ASP535
|
4.1
|
27.1
|
1.0
|
C
|
A:ASP678
|
4.1
|
30.4
|
1.0
|
CA
|
A:ASP535
|
4.2
|
26.8
|
1.0
|
CA
|
A:LEU534
|
4.2
|
26.4
|
1.0
|
CA
|
A:ASP533
|
4.3
|
25.5
|
1.0
|
CA
|
A:ASP678
|
4.4
|
30.6
|
1.0
|
OD2
|
A:ASP533
|
4.4
|
26.4
|
1.0
|
OD2
|
A:ASP678
|
4.4
|
32.9
|
1.0
|
N
|
A:VAL680
|
4.5
|
27.9
|
1.0
|
O
|
A:ASP533
|
4.5
|
24.7
|
1.0
|
CB
|
A:ASP533
|
4.6
|
26.1
|
1.0
|
CB
|
A:ASP535
|
4.6
|
26.3
|
1.0
|
OD2
|
A:ASP535
|
4.6
|
25.8
|
1.0
|
CB
|
A:ASP678
|
4.6
|
31.2
|
1.0
|
O
|
A:GLU539
|
4.7
|
31.4
|
1.0
|
CE
|
A:LYS133
|
4.8
|
28.2
|
1.0
|
CG2
|
A:VAL680
|
4.8
|
28.3
|
1.0
|
CA
|
A:VAL680
|
4.9
|
28.4
|
1.0
|
CB
|
A:GLU539
|
4.9
|
32.8
|
1.0
|
CB
|
A:ALA679
|
4.9
|
29.6
|
1.0
|
O
|
A:ASP678
|
5.0
|
29.6
|
1.0
|
|
Sodium binding site 3 out
of 4 in 2wof
Go back to
Sodium Binding Sites List in 2wof
Sodium binding site 3 out
of 4 in the Edta Treated E. Coli Copper Amine Oxidase
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 3 of Edta Treated E. Coli Copper Amine Oxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na1728
b:36.7
occ:1.00
|
OE2
|
B:GLU573
|
2.2
|
32.7
|
1.0
|
O
|
B:TYR667
|
2.4
|
36.6
|
1.0
|
OE2
|
B:GLU672
|
2.6
|
50.6
|
1.0
|
O
|
B:HOH2417
|
2.7
|
43.2
|
1.0
|
OE1
|
B:GLU573
|
2.7
|
34.2
|
1.0
|
O
|
B:HOH2378
|
2.8
|
47.5
|
1.0
|
CD
|
B:GLU573
|
2.8
|
38.1
|
1.0
|
CD
|
B:GLU672
|
3.5
|
49.9
|
1.0
|
C
|
B:TYR667
|
3.6
|
37.6
|
1.0
|
CG
|
B:GLU672
|
3.7
|
46.1
|
1.0
|
CG
|
B:GLU573
|
4.3
|
39.2
|
1.0
|
CA
|
B:SER668
|
4.4
|
38.2
|
1.0
|
CB
|
B:GLU672
|
4.4
|
42.7
|
1.0
|
N
|
B:ARG642
|
4.4
|
35.8
|
1.0
|
OE1
|
B:GLU647
|
4.5
|
39.9
|
1.0
|
N
|
B:SER668
|
4.5
|
37.5
|
1.0
|
CA
|
B:TYR667
|
4.5
|
37.3
|
1.0
|
CB
|
B:THR641
|
4.6
|
34.7
|
1.0
|
CB
|
B:ARG642
|
4.6
|
37.3
|
1.0
|
OE1
|
B:GLU672
|
4.7
|
51.2
|
1.0
|
OE2
|
B:GLU647
|
4.8
|
43.0
|
1.0
|
CG2
|
B:THR641
|
4.9
|
37.9
|
1.0
|
CB
|
B:TYR667
|
4.9
|
36.8
|
1.0
|
O
|
B:ARG642
|
5.0
|
36.2
|
1.0
|
|
Sodium binding site 4 out
of 4 in 2wof
Go back to
Sodium Binding Sites List in 2wof
Sodium binding site 4 out
of 4 in the Edta Treated E. Coli Copper Amine Oxidase
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 4 of Edta Treated E. Coli Copper Amine Oxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na1729
b:30.2
occ:1.00
|
OD1
|
B:ASP533
|
2.2
|
27.9
|
1.0
|
O
|
B:ALA679
|
2.3
|
31.2
|
1.0
|
O
|
B:LEU534
|
2.4
|
27.0
|
1.0
|
OD1
|
B:ASP535
|
2.4
|
31.6
|
1.0
|
OD1
|
B:ASP678
|
2.5
|
31.3
|
1.0
|
O
|
B:HOH2353
|
2.5
|
29.2
|
1.0
|
C
|
B:LEU534
|
3.3
|
28.4
|
1.0
|
C
|
B:ALA679
|
3.4
|
31.4
|
1.0
|
N
|
B:ALA679
|
3.5
|
32.6
|
1.0
|
CG
|
B:ASP533
|
3.5
|
28.0
|
1.0
|
NZ
|
B:LYS133
|
3.6
|
30.7
|
1.0
|
CG
|
B:ASP535
|
3.6
|
29.6
|
1.0
|
N
|
B:LEU534
|
3.7
|
28.5
|
1.0
|
CG
|
B:ASP678
|
3.7
|
32.9
|
1.0
|
C
|
B:ASP533
|
3.9
|
28.2
|
1.0
|
CA
|
B:ALA679
|
4.0
|
31.7
|
1.0
|
N
|
B:ASP535
|
4.0
|
28.5
|
1.0
|
CA
|
B:LEU534
|
4.1
|
27.9
|
1.0
|
C
|
B:ASP678
|
4.2
|
33.1
|
1.0
|
CA
|
B:ASP535
|
4.3
|
28.9
|
1.0
|
CA
|
B:ASP533
|
4.3
|
27.6
|
1.0
|
OD2
|
B:ASP533
|
4.3
|
25.8
|
1.0
|
O
|
B:ASP533
|
4.4
|
28.8
|
1.0
|
OD2
|
B:ASP678
|
4.4
|
33.3
|
1.0
|
OD2
|
B:ASP535
|
4.5
|
29.8
|
1.0
|
N
|
B:VAL680
|
4.5
|
31.4
|
1.0
|
CA
|
B:ASP678
|
4.5
|
32.2
|
1.0
|
CB
|
B:ASP533
|
4.5
|
27.9
|
1.0
|
CB
|
B:ASP535
|
4.6
|
29.4
|
1.0
|
CB
|
B:ASP678
|
4.7
|
32.5
|
1.0
|
CB
|
B:ALA679
|
4.8
|
31.9
|
1.0
|
O
|
B:GLU539
|
4.8
|
35.7
|
1.0
|
CA
|
B:VAL680
|
4.8
|
31.5
|
1.0
|
CE
|
B:LYS133
|
4.9
|
32.3
|
1.0
|
CG2
|
B:VAL680
|
4.9
|
32.1
|
1.0
|
|
Reference:
M.A.Smith,
P.Pirrat,
A.R.Pearson,
C.R.Kurtis,
T.G.Gaule,
P.F.Knowles,
S.E.Phillips,
M.J.Mcpherson.
Exploring the Roles of the Metal Ions in Escherichia Coli Copper Amine Oxidase. Biochemistry V. 49 1268 2010.
ISSN: ISSN 0006-2960
PubMed: 20052994
DOI: 10.1021/BI901738K
Page generated: Mon Oct 7 04:44:28 2024
|