Manganese in PDB 2nym: Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit
Enzymatic activity of Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit
All present enzymatic activity of Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit:
3.1.3.16;
Protein crystallography data
The structure of Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit, PDB code: 2nym
was solved by
Y.Chen,
Y.Xing,
Y.Xu,
Y.Chao,
Z.Lin,
P.D.Jeffrey,
Y.Shi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
100.00 /
3.60
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
108.170,
158.860,
270.750,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
26.7 /
33.1
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit
(pdb code 2nym). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the
Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit, PDB code: 2nym:
Jump to Manganese binding site number:
1;
2;
3;
4;
Manganese binding site 1 out
of 4 in 2nym
Go back to
Manganese Binding Sites List in 2nym
Manganese binding site 1 out
of 4 in the Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn501
b:23.7
occ:1.00
|
OD1
|
C:ASN117
|
2.0
|
24.5
|
1.0
|
ND1
|
C:HIS241
|
2.1
|
64.8
|
1.0
|
NE2
|
C:HIS167
|
2.1
|
21.9
|
1.0
|
OD2
|
C:ASP85
|
2.2
|
50.7
|
1.0
|
CE1
|
C:HIS167
|
2.5
|
25.7
|
1.0
|
CE1
|
C:HIS241
|
2.7
|
72.7
|
1.0
|
CG
|
C:ASN117
|
2.7
|
25.1
|
1.0
|
CG
|
C:ASP85
|
2.8
|
47.0
|
1.0
|
MN
|
C:MN502
|
2.9
|
60.0
|
1.0
|
ND2
|
C:ASN117
|
2.9
|
5.5
|
1.0
|
OD1
|
C:ASP85
|
2.9
|
38.8
|
1.0
|
CG
|
C:HIS241
|
3.4
|
66.8
|
1.0
|
OD2
|
C:ASP57
|
3.4
|
50.4
|
1.0
|
CD2
|
C:HIS167
|
3.4
|
29.2
|
1.0
|
O
|
C:HIS241
|
3.8
|
52.5
|
1.0
|
ND1
|
C:HIS167
|
3.8
|
34.7
|
1.0
|
CA
|
C:HIS241
|
4.0
|
50.8
|
1.0
|
CB
|
C:HIS241
|
4.0
|
58.2
|
1.0
|
NE2
|
C:HIS241
|
4.0
|
70.0
|
1.0
|
CD2
|
C:HIS118
|
4.2
|
45.2
|
1.0
|
CB
|
C:ASN117
|
4.2
|
26.8
|
1.0
|
CB
|
C:ASP85
|
4.2
|
50.0
|
1.0
|
CG
|
C:ASP57
|
4.3
|
46.9
|
1.0
|
CG
|
C:HIS167
|
4.3
|
37.3
|
1.0
|
CD2
|
C:HIS241
|
4.3
|
68.3
|
1.0
|
C
|
C:HIS241
|
4.3
|
48.7
|
1.0
|
OD1
|
C:ASP57
|
4.4
|
42.5
|
1.0
|
N
|
C:ASN117
|
4.6
|
43.4
|
1.0
|
NE2
|
C:HIS59
|
4.6
|
52.2
|
1.0
|
NE2
|
C:HIS118
|
4.8
|
46.8
|
1.0
|
OXT
|
G:FGA6
|
4.8
|
95.7
|
1.0
|
CE1
|
C:HIS59
|
4.9
|
47.9
|
1.0
|
CA
|
C:ASN117
|
5.0
|
39.6
|
1.0
|
|
Manganese binding site 2 out
of 4 in 2nym
Go back to
Manganese Binding Sites List in 2nym
Manganese binding site 2 out
of 4 in the Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn502
b:60.0
occ:1.00
|
OD2
|
C:ASP85
|
2.0
|
50.7
|
1.0
|
OD2
|
C:ASP57
|
2.2
|
50.4
|
1.0
|
NE2
|
C:HIS59
|
2.3
|
52.2
|
1.0
|
MN
|
C:MN501
|
2.9
|
23.7
|
1.0
|
CE1
|
C:HIS59
|
3.2
|
47.9
|
1.0
|
CG
|
C:ASP85
|
3.2
|
47.0
|
1.0
|
OXT
|
G:FGA6
|
3.3
|
95.7
|
1.0
|
CD2
|
C:HIS59
|
3.4
|
48.1
|
1.0
|
CG
|
C:ASP57
|
3.4
|
46.9
|
1.0
|
OH
|
C:TYR265
|
3.7
|
27.4
|
1.0
|
CE1
|
C:PHE260
|
4.0
|
45.3
|
1.0
|
CB
|
C:ASP85
|
4.1
|
50.0
|
1.0
|
OD1
|
C:ASP85
|
4.2
|
38.8
|
1.0
|
O
|
C:HIS241
|
4.3
|
52.5
|
1.0
|
CB
|
C:ASP57
|
4.3
|
45.2
|
1.0
|
OD1
|
C:ASP57
|
4.3
|
42.5
|
1.0
|
ND1
|
C:HIS59
|
4.3
|
42.8
|
1.0
|
C
|
G:FGA6
|
4.4
|
91.2
|
1.0
|
CD2
|
C:HIS118
|
4.4
|
45.2
|
1.0
|
NE2
|
C:HIS118
|
4.4
|
46.8
|
1.0
|
ND1
|
C:HIS241
|
4.4
|
64.8
|
1.0
|
CE1
|
C:HIS167
|
4.5
|
25.7
|
1.0
|
CG
|
C:HIS59
|
4.5
|
42.8
|
1.0
|
CZ
|
C:PHE260
|
4.5
|
45.3
|
1.0
|
CZ
|
C:TYR265
|
4.5
|
31.6
|
1.0
|
O
|
G:FGA6
|
4.6
|
93.2
|
1.0
|
OD1
|
C:ASN117
|
4.6
|
24.5
|
1.0
|
ND2
|
C:ASN117
|
4.7
|
5.5
|
1.0
|
NE2
|
C:HIS167
|
4.7
|
21.9
|
1.0
|
C
|
C:HIS241
|
4.7
|
48.7
|
1.0
|
CA
|
C:HIS241
|
4.9
|
50.8
|
1.0
|
|
Manganese binding site 3 out
of 4 in 2nym
Go back to
Manganese Binding Sites List in 2nym
Manganese binding site 3 out
of 4 in the Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mn501
b:30.7
occ:1.00
|
OD1
|
F:ASN117
|
2.0
|
18.0
|
1.0
|
ND1
|
F:HIS241
|
2.1
|
38.5
|
1.0
|
NE2
|
F:HIS167
|
2.2
|
9.5
|
1.0
|
OD2
|
F:ASP85
|
2.3
|
30.5
|
1.0
|
CE1
|
F:HIS167
|
2.6
|
13.9
|
1.0
|
CE1
|
F:HIS241
|
2.7
|
43.5
|
1.0
|
MN
|
F:MN502
|
2.7
|
33.5
|
1.0
|
CG
|
F:ASN117
|
2.7
|
14.8
|
1.0
|
ND2
|
F:ASN117
|
2.9
|
4.6
|
1.0
|
CG
|
F:ASP85
|
3.1
|
29.1
|
1.0
|
OD1
|
F:ASP85
|
3.3
|
18.7
|
1.0
|
CG
|
F:HIS241
|
3.4
|
43.5
|
1.0
|
CD2
|
F:HIS167
|
3.5
|
13.8
|
1.0
|
OD2
|
F:ASP57
|
3.5
|
35.7
|
1.0
|
O
|
F:HIS241
|
3.7
|
40.2
|
1.0
|
ND1
|
F:HIS167
|
3.9
|
18.7
|
1.0
|
CA
|
F:HIS241
|
3.9
|
38.7
|
1.0
|
NE2
|
F:HIS241
|
4.0
|
35.8
|
1.0
|
CB
|
F:HIS241
|
4.0
|
42.0
|
1.0
|
CB
|
F:ASN117
|
4.2
|
20.1
|
1.0
|
C
|
F:HIS241
|
4.2
|
40.2
|
1.0
|
CD2
|
F:HIS118
|
4.2
|
42.0
|
1.0
|
CD2
|
F:HIS241
|
4.3
|
41.5
|
1.0
|
CG
|
F:HIS167
|
4.4
|
17.3
|
1.0
|
CB
|
F:ASP85
|
4.4
|
34.9
|
1.0
|
CG
|
F:ASP57
|
4.4
|
38.8
|
1.0
|
OD1
|
F:ASP57
|
4.6
|
39.8
|
1.0
|
N
|
F:ASN117
|
4.6
|
28.1
|
1.0
|
NE2
|
F:HIS59
|
4.6
|
39.3
|
1.0
|
OXT
|
H:FGA6
|
4.7
|
79.9
|
1.0
|
NE2
|
F:HIS118
|
4.7
|
47.7
|
1.0
|
O3
|
H:1ZN5
|
4.9
|
60.9
|
1.0
|
CE1
|
F:HIS59
|
5.0
|
40.3
|
1.0
|
CA
|
F:ASN117
|
5.0
|
30.3
|
1.0
|
|
Manganese binding site 4 out
of 4 in 2nym
Go back to
Manganese Binding Sites List in 2nym
Manganese binding site 4 out
of 4 in the Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Crystal Structure of Protein Phosphatase 2A (PP2A) with C-Terminus Truncated Catalytic Subunit within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mn502
b:33.5
occ:1.00
|
OD2
|
F:ASP85
|
2.0
|
30.5
|
1.0
|
OD2
|
F:ASP57
|
2.2
|
35.7
|
1.0
|
NE2
|
F:HIS59
|
2.3
|
39.3
|
1.0
|
MN
|
F:MN501
|
2.7
|
30.7
|
1.0
|
CE1
|
F:HIS59
|
3.1
|
40.3
|
1.0
|
CG
|
F:ASP85
|
3.2
|
29.1
|
1.0
|
OXT
|
H:FGA6
|
3.4
|
79.9
|
1.0
|
CD2
|
F:HIS59
|
3.4
|
39.7
|
1.0
|
CG
|
F:ASP57
|
3.4
|
38.8
|
1.0
|
OH
|
F:TYR265
|
3.6
|
20.9
|
1.0
|
CB
|
F:ASP85
|
4.0
|
34.9
|
1.0
|
OD1
|
F:ASP85
|
4.1
|
18.7
|
1.0
|
CE1
|
F:PHE260
|
4.2
|
30.6
|
1.0
|
O
|
F:HIS241
|
4.2
|
40.2
|
1.0
|
NE2
|
F:HIS118
|
4.2
|
47.7
|
1.0
|
CD2
|
F:HIS118
|
4.2
|
42.0
|
1.0
|
OD1
|
F:ASP57
|
4.3
|
39.8
|
1.0
|
CE1
|
F:HIS167
|
4.3
|
13.9
|
1.0
|
C
|
H:FGA6
|
4.3
|
75.6
|
1.0
|
ND1
|
F:HIS59
|
4.3
|
37.9
|
1.0
|
CB
|
F:ASP57
|
4.3
|
35.9
|
1.0
|
O
|
H:FGA6
|
4.4
|
81.2
|
1.0
|
CG
|
F:HIS59
|
4.5
|
36.9
|
1.0
|
ND1
|
F:HIS241
|
4.5
|
38.5
|
1.0
|
OD1
|
F:ASN117
|
4.5
|
18.0
|
1.0
|
CZ
|
F:TYR265
|
4.5
|
17.9
|
1.0
|
ND2
|
F:ASN117
|
4.5
|
4.6
|
1.0
|
NE2
|
F:HIS167
|
4.6
|
9.5
|
1.0
|
CZ
|
F:PHE260
|
4.6
|
33.2
|
1.0
|
C
|
F:HIS241
|
4.8
|
40.2
|
1.0
|
O3
|
H:1ZN5
|
4.8
|
60.9
|
1.0
|
CG
|
F:ASN117
|
5.0
|
14.8
|
1.0
|
CA
|
F:HIS241
|
5.0
|
38.7
|
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 14:41:00 2024
|