Manganese in PDB 2npp: Structure of the Protein Phosphatase 2A Holoenzyme
Enzymatic activity of Structure of the Protein Phosphatase 2A Holoenzyme
All present enzymatic activity of Structure of the Protein Phosphatase 2A Holoenzyme:
3.1.3.16;
Protein crystallography data
The structure of Structure of the Protein Phosphatase 2A Holoenzyme, PDB code: 2npp
was solved by
Y.Xu,
Y.Chen,
Y.Xing,
Y.Chao,
Y.Shi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
100.00 /
3.30
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
109.260,
159.050,
269.170,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
25.5 /
29.9
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Structure of the Protein Phosphatase 2A Holoenzyme
(pdb code 2npp). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the
Structure of the Protein Phosphatase 2A Holoenzyme, PDB code: 2npp:
Jump to Manganese binding site number:
1;
2;
3;
4;
Manganese binding site 1 out
of 4 in 2npp
Go back to
Manganese Binding Sites List in 2npp
Manganese binding site 1 out
of 4 in the Structure of the Protein Phosphatase 2A Holoenzyme
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Structure of the Protein Phosphatase 2A Holoenzyme within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn501
b:46.3
occ:1.00
|
OD1
|
C:ASN117
|
2.0
|
48.8
|
1.0
|
ND1
|
C:HIS241
|
2.1
|
67.1
|
1.0
|
NE2
|
C:HIS167
|
2.1
|
43.4
|
1.0
|
OD2
|
C:ASP85
|
2.2
|
59.1
|
1.0
|
CE1
|
C:HIS167
|
2.5
|
49.3
|
1.0
|
CE1
|
C:HIS241
|
2.6
|
74.6
|
1.0
|
MN
|
C:MN502
|
2.7
|
65.3
|
1.0
|
CG
|
C:ASP85
|
3.0
|
56.6
|
1.0
|
CG
|
C:ASN117
|
3.0
|
46.7
|
1.0
|
OD1
|
C:ASP85
|
3.2
|
49.8
|
1.0
|
CG
|
C:HIS241
|
3.3
|
72.5
|
1.0
|
ND2
|
C:ASN117
|
3.3
|
35.8
|
1.0
|
CD2
|
C:HIS167
|
3.4
|
48.1
|
1.0
|
OD2
|
C:ASP57
|
3.6
|
49.4
|
1.0
|
O
|
C:HIS241
|
3.6
|
69.4
|
1.0
|
ND1
|
C:HIS167
|
3.8
|
51.5
|
1.0
|
NE2
|
C:HIS241
|
3.8
|
70.8
|
1.0
|
CA
|
C:HIS241
|
3.9
|
66.3
|
1.0
|
CB
|
C:HIS241
|
4.0
|
68.0
|
1.0
|
CD2
|
C:HIS241
|
4.2
|
71.3
|
1.0
|
C
|
C:HIS241
|
4.2
|
67.8
|
1.0
|
CD2
|
C:HIS118
|
4.2
|
51.3
|
1.0
|
CB
|
C:ASP85
|
4.3
|
56.3
|
1.0
|
CG
|
C:HIS167
|
4.3
|
51.1
|
1.0
|
CB
|
C:ASN117
|
4.3
|
45.5
|
1.0
|
OD1
|
C:ASP57
|
4.4
|
50.0
|
1.0
|
CG
|
C:ASP57
|
4.4
|
52.4
|
1.0
|
NE2
|
C:HIS59
|
4.6
|
57.8
|
1.0
|
N
|
C:ASN117
|
4.7
|
52.9
|
1.0
|
NE2
|
C:HIS118
|
4.8
|
55.5
|
1.0
|
|
Manganese binding site 2 out
of 4 in 2npp
Go back to
Manganese Binding Sites List in 2npp
Manganese binding site 2 out
of 4 in the Structure of the Protein Phosphatase 2A Holoenzyme
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Structure of the Protein Phosphatase 2A Holoenzyme within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn502
b:65.3
occ:1.00
|
OD2
|
C:ASP85
|
2.0
|
59.1
|
1.0
|
OD2
|
C:ASP57
|
2.1
|
49.4
|
1.0
|
NE2
|
C:HIS59
|
2.3
|
57.8
|
1.0
|
MN
|
C:MN501
|
2.7
|
46.3
|
1.0
|
CE1
|
C:HIS59
|
3.1
|
55.1
|
1.0
|
CG
|
C:ASP85
|
3.2
|
56.6
|
1.0
|
CG
|
C:ASP57
|
3.4
|
52.4
|
1.0
|
CD2
|
C:HIS59
|
3.4
|
56.3
|
1.0
|
OH
|
C:TYR265
|
3.9
|
55.5
|
1.0
|
CB
|
C:ASP85
|
4.0
|
56.3
|
1.0
|
CD2
|
C:HIS118
|
4.0
|
51.3
|
1.0
|
O
|
C:HIS241
|
4.0
|
69.4
|
1.0
|
OD1
|
C:ASP57
|
4.1
|
50.0
|
1.0
|
OD1
|
C:ASP85
|
4.1
|
49.8
|
1.0
|
NE2
|
C:HIS118
|
4.2
|
55.5
|
1.0
|
OD1
|
C:ASN117
|
4.2
|
48.8
|
1.0
|
ND1
|
C:HIS59
|
4.3
|
49.7
|
1.0
|
CE1
|
C:HIS167
|
4.3
|
49.3
|
1.0
|
CB
|
C:ASP57
|
4.4
|
50.9
|
1.0
|
CE1
|
C:PHE260
|
4.4
|
51.3
|
1.0
|
CG
|
C:HIS59
|
4.5
|
50.9
|
1.0
|
ND1
|
C:HIS241
|
4.5
|
67.1
|
1.0
|
NE2
|
C:HIS167
|
4.6
|
43.4
|
1.0
|
C
|
C:HIS241
|
4.6
|
67.8
|
1.0
|
C
|
X:FGA6
|
4.7
|
97.2
|
1.0
|
CZ
|
C:TYR265
|
4.7
|
51.6
|
1.0
|
ND2
|
C:ASN117
|
4.8
|
35.8
|
1.0
|
CA
|
C:HIS241
|
4.9
|
66.3
|
1.0
|
O3
|
X:1ZN5
|
4.9
|
89.8
|
1.0
|
CE1
|
C:HIS241
|
5.0
|
74.6
|
1.0
|
CG
|
C:ASN117
|
5.0
|
46.7
|
1.0
|
|
Manganese binding site 3 out
of 4 in 2npp
Go back to
Manganese Binding Sites List in 2npp
Manganese binding site 3 out
of 4 in the Structure of the Protein Phosphatase 2A Holoenzyme
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Structure of the Protein Phosphatase 2A Holoenzyme within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mn501
b:35.5
occ:1.00
|
OD1
|
F:ASN117
|
2.0
|
46.6
|
1.0
|
ND1
|
F:HIS241
|
2.1
|
72.9
|
1.0
|
NE2
|
F:HIS167
|
2.2
|
37.8
|
1.0
|
CE1
|
F:HIS241
|
2.6
|
78.6
|
1.0
|
OD2
|
F:ASP85
|
2.6
|
57.7
|
1.0
|
CE1
|
F:HIS167
|
2.7
|
43.2
|
1.0
|
MN
|
F:MN502
|
2.9
|
56.7
|
1.0
|
CG
|
F:ASN117
|
3.0
|
42.6
|
1.0
|
CG
|
F:ASP85
|
3.1
|
54.1
|
1.0
|
OD1
|
F:ASP85
|
3.1
|
48.9
|
1.0
|
ND2
|
F:ASN117
|
3.3
|
40.4
|
1.0
|
CG
|
F:HIS241
|
3.3
|
77.8
|
1.0
|
CD2
|
F:HIS167
|
3.4
|
42.9
|
1.0
|
O
|
F:HIS241
|
3.6
|
63.9
|
1.0
|
OD2
|
F:ASP57
|
3.8
|
55.3
|
1.0
|
NE2
|
F:HIS241
|
3.8
|
75.7
|
1.0
|
CA
|
F:HIS241
|
4.0
|
63.6
|
1.0
|
ND1
|
F:HIS167
|
4.0
|
45.8
|
1.0
|
CB
|
F:HIS241
|
4.1
|
71.7
|
1.0
|
CD2
|
F:HIS241
|
4.2
|
75.9
|
1.0
|
CD2
|
F:HIS118
|
4.2
|
50.7
|
1.0
|
C
|
F:HIS241
|
4.2
|
61.6
|
1.0
|
CB
|
F:ASN117
|
4.3
|
41.1
|
1.0
|
CG
|
F:HIS167
|
4.4
|
41.1
|
1.0
|
CB
|
F:ASP85
|
4.4
|
58.1
|
1.0
|
OD1
|
F:ASP57
|
4.5
|
56.9
|
1.0
|
CG
|
F:ASP57
|
4.6
|
55.5
|
1.0
|
N
|
F:ASN117
|
4.6
|
46.8
|
1.0
|
NE2
|
F:HIS118
|
4.8
|
54.2
|
1.0
|
NE2
|
F:HIS59
|
4.8
|
53.8
|
1.0
|
CA
|
F:ASN117
|
5.0
|
46.3
|
1.0
|
|
Manganese binding site 4 out
of 4 in 2npp
Go back to
Manganese Binding Sites List in 2npp
Manganese binding site 4 out
of 4 in the Structure of the Protein Phosphatase 2A Holoenzyme
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Structure of the Protein Phosphatase 2A Holoenzyme within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mn502
b:56.7
occ:1.00
|
OD2
|
F:ASP85
|
2.0
|
57.7
|
1.0
|
OD2
|
F:ASP57
|
2.2
|
55.3
|
1.0
|
NE2
|
F:HIS59
|
2.3
|
53.8
|
1.0
|
MN
|
F:MN501
|
2.9
|
35.5
|
1.0
|
CE1
|
F:HIS59
|
3.1
|
51.9
|
1.0
|
CG
|
F:ASP85
|
3.2
|
54.1
|
1.0
|
CD2
|
F:HIS59
|
3.4
|
51.2
|
1.0
|
CG
|
F:ASP57
|
3.4
|
55.5
|
1.0
|
OH
|
F:TYR265
|
4.0
|
50.3
|
1.0
|
CD2
|
F:HIS118
|
4.1
|
50.7
|
1.0
|
OD1
|
F:ASP85
|
4.1
|
48.9
|
1.0
|
CB
|
F:ASP85
|
4.1
|
58.1
|
1.0
|
O
|
F:HIS241
|
4.1
|
63.9
|
1.0
|
OD1
|
F:ASP57
|
4.1
|
56.9
|
1.0
|
NE2
|
F:HIS118
|
4.2
|
54.2
|
1.0
|
ND1
|
F:HIS59
|
4.3
|
45.1
|
1.0
|
OD1
|
F:ASN117
|
4.4
|
46.6
|
1.0
|
CB
|
F:ASP57
|
4.4
|
52.7
|
1.0
|
CE1
|
F:HIS167
|
4.4
|
43.2
|
1.0
|
CE1
|
F:PHE260
|
4.5
|
64.7
|
1.0
|
CG
|
F:HIS59
|
4.5
|
44.0
|
1.0
|
C
|
Y:FGA6
|
4.6
|
93.3
|
1.0
|
NE2
|
F:HIS167
|
4.6
|
37.8
|
1.0
|
ND1
|
F:HIS241
|
4.6
|
72.9
|
1.0
|
CZ
|
F:TYR265
|
4.7
|
48.0
|
1.0
|
C
|
F:HIS241
|
4.8
|
61.6
|
1.0
|
O3
|
Y:1ZN5
|
4.8
|
78.5
|
1.0
|
CZ
|
F:PHE260
|
5.0
|
63.9
|
1.0
|
|
Reference:
Y.Xu,
Y.Xing,
Y.Chen,
Y.Chao,
Z.Lin,
E.Fan,
J.W.Yu,
S.Strack,
P.D.Jeffrey,
Y.Shi.
Structure of the Protein Phosphatase 2A Holoenzyme Cell(Cambridge,Mass.) V. 127 1239 2006.
ISSN: ISSN 0092-8674
PubMed: 17174897
DOI: 10.1016/J.CELL.2006.11.033
Page generated: Sat Oct 5 14:39:02 2024
|