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Manganese in PDB 2ie3: Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor- Inducing Toxins

Enzymatic activity of Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor- Inducing Toxins

All present enzymatic activity of Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor- Inducing Toxins:
3.1.3.16;

Protein crystallography data

The structure of Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor- Inducing Toxins, PDB code: 2ie3 was solved by Y.Xing, Y.Xu, Y.Chen, P.D.Jeffrey, Y.Chao, Y.Shi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.80
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.070, 195.090, 201.910, 90.00, 90.00, 90.00
R / Rfree (%) 22.1 / 26.4

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor- Inducing Toxins (pdb code 2ie3). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor- Inducing Toxins, PDB code: 2ie3:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 2ie3

Go back to Manganese Binding Sites List in 2ie3
Manganese binding site 1 out of 2 in the Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor- Inducing Toxins


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 Core Enzyme Bound to Tumor- Inducing Toxins within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn501

b:37.6
occ:1.00
OD1 C:ASN117 2.0 39.0 1.0
NE2 C:HIS167 2.1 36.4 1.0
ND1 C:HIS241 2.1 43.8 1.0
OD2 C:ASP85 2.7 34.9 1.0
CG C:ASN117 2.9 43.0 1.0
CE1 C:HIS167 2.9 28.6 1.0
CE1 C:HIS241 3.0 45.0 1.0
CG C:HIS241 3.2 43.9 1.0
MN C:MN502 3.2 46.0 1.0
CD2 C:HIS167 3.2 38.6 1.0
CG C:ASP85 3.3 39.7 1.0
ND2 C:ASN117 3.3 45.5 1.0
OD1 C:ASP85 3.3 38.8 1.0
CA C:HIS241 3.6 39.0 1.0
CB C:HIS241 3.6 40.8 1.0
OD2 C:ASP57 3.9 34.5 1.0
O C:HIS241 4.0 41.0 1.0
ND1 C:HIS167 4.1 32.6 1.0
NE2 C:HIS241 4.1 37.7 1.0
CB C:ASN117 4.2 40.6 1.0
CD2 C:HIS241 4.2 39.3 1.0
C C:HIS241 4.3 40.7 1.0
CG C:HIS167 4.3 34.9 1.0
CD2 C:HIS118 4.3 28.9 1.0
N C:ASN117 4.5 39.1 1.0
CB C:ASP85 4.6 42.1 1.0
N C:HIS241 4.6 38.6 1.0
NH1 C:ARG214 4.7 37.8 1.0
CG C:ASP57 4.8 44.4 1.0
O C:LEU199 4.9 45.6 1.0
CA C:ASN117 4.9 41.9 1.0
OD1 C:ASP57 4.9 45.8 1.0
NE2 C:HIS118 5.0 30.7 1.0

Manganese binding site 2 out of 2 in 2ie3

Go back to Manganese Binding Sites List in 2ie3
Manganese binding site 2 out of 2 in the Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor- Inducing Toxins


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 Core Enzyme Bound to Tumor- Inducing Toxins within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn502

b:46.0
occ:1.00
OD2 C:ASP85 2.0 34.9 1.0
OD2 C:ASP57 2.1 34.5 1.0
NE2 C:HIS59 2.3 45.8 1.0
MN C:MN501 3.2 37.6 1.0
CE1 C:HIS59 3.2 40.0 1.0
CG C:ASP85 3.2 39.7 1.0
CD2 C:HIS59 3.3 38.7 1.0
CG C:ASP57 3.4 44.4 1.0
O I:FGA6 4.0 51.4 1.0
CB C:ASP85 4.1 42.1 1.0
CD2 C:HIS118 4.1 28.9 1.0
OH C:TYR265 4.1 31.7 1.0
OD1 C:ASP85 4.2 38.8 1.0
CB C:ASP57 4.2 45.3 1.0
CE1 C:PHE260 4.2 45.8 1.0
O C:HIS241 4.2 41.0 1.0
OD1 C:ASP57 4.3 45.8 1.0
NE2 C:HIS118 4.4 30.7 1.0
ND1 C:HIS59 4.4 43.7 1.0
CG C:HIS59 4.5 44.6 1.0
CE1 C:HIS167 4.5 28.6 1.0
CA C:HIS241 4.5 39.0 1.0
OD1 C:ASN117 4.6 39.0 1.0
NE2 C:HIS167 4.6 36.4 1.0
C C:HIS241 4.7 40.7 1.0
CZ C:PHE260 4.7 46.3 1.0
CZ C:TYR265 4.8 32.2 1.0
C I:FGA6 4.8 52.9 1.0
ND1 C:HIS241 4.9 43.8 1.0
OXT I:FGA6 4.9 59.5 1.0

Reference:

Y.Xing, Y.Xu, Y.Chen, P.D.Jeffrey, Y.Chao, Z.Lin, Z.Li, S.Strack, J.B.Stock, Y.Shi. Structure of Protein Phosphatase 2A Core Enzyme Bound to Tumor-Inducing Toxins Cell(Cambridge,Mass.) V. 127 341 2006.
ISSN: ISSN 0092-8674
PubMed: 17055435
DOI: 10.1016/J.CELL.2006.09.025
Page generated: Tue Dec 15 04:02:50 2020

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