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Manganese in PDB 2nyl: Crystal Structure of Protein Phosphatase 2A (PP2A) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated

Enzymatic activity of Crystal Structure of Protein Phosphatase 2A (PP2A) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated

All present enzymatic activity of Crystal Structure of Protein Phosphatase 2A (PP2A) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated:
3.1.3.16;

Protein crystallography data

The structure of Crystal Structure of Protein Phosphatase 2A (PP2A) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated, PDB code: 2nyl was solved by Y.Xing, Y.Xu, Y.Chen, Y.Chao, Z.Lin, Y.Shi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 3.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 108.480, 159.850, 270.370, 90.00, 90.00, 90.00
R / Rfree (%) 28.2 / 33.5

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Protein Phosphatase 2A (PP2A) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated (pdb code 2nyl). 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) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated, PDB code: 2nyl:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 2nyl

Go back to Manganese Binding Sites List in 2nyl
Manganese binding site 1 out of 4 in the Crystal Structure of Protein Phosphatase 2A (PP2A) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated


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) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn501

b:59.6
occ:1.00
 OD1 C:ASN117 2.0 47.9 1.0
ND1 C:HIS241 2.1 76.3 1.0
NE2 C:HIS167 2.2 57.1 1.0
OD2 C:ASP85 2.3 58.9 1.0
CE1 C:HIS241 2.5 80.3 1.0
CG C:ASN117 2.6 44.7 1.0
ND2 C:ASN117 2.7 38.8 1.0
CE1 C:HIS167 2.7 57.6 1.0
MN C:MN502 2.7 60.9 1.0
CG C:ASP85 3.0 56.0 1.0
OD1 C:ASP85 3.2 51.3 1.0
CG C:HIS241 3.4 76.4 1.0
CD2 C:HIS167 3.5 58.9 1.0
OD2 C:ASP57 3.7 61.1 1.0
O C:HIS241 3.7 67.2 1.0
NE2 C:HIS241 3.8 77.8 1.0
ND1 C:HIS167 4.0 60.3 1.0
CB C:ASN117 4.0 44.2 1.0
CD2 C:HIS118 4.2 46.8 1.0
CB C:HIS241 4.2 71.8 1.0
CA C:HIS241 4.2 67.8 1.0
CD2 C:HIS241 4.3 76.3 1.0
CG C:HIS167 4.4 61.4 1.0
C C:HIS241 4.4 66.6 1.0
CB C:ASP85 4.4 55.9 1.0
NE2 C:HIS59 4.6 57.3 1.0
CG C:ASP57 4.6 58.6 1.0
N C:ASN117 4.7 47.7 1.0
OD1 C:ASP57 4.7 56.5 1.0
O G:FGA6 4.8 0.6 1.0
NE2 C:HIS118 4.8 45.2 1.0
O3 G:1ZN5 4.8 0.1 1.0
CE1 C:HIS59 4.8 56.3 1.0
CA C:ASN117 4.9 46.1 1.0

Manganese binding site 2 out of 4 in 2nyl

Go back to Manganese Binding Sites List in 2nyl
Manganese binding site 2 out of 4 in the Crystal Structure of Protein Phosphatase 2A (PP2A) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated


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) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn502

b:60.9
occ:1.00
 OD2 C:ASP85 2.0 58.9 1.0
OD2 C:ASP57 2.2 61.1 1.0
NE2 C:HIS59 2.3 57.3 1.0
MN C:MN501 2.7 59.6 1.0
CE1 C:HIS59 3.2 56.3 1.0
CG C:ASP85 3.2 56.0 1.0
CD2 C:HIS59 3.4 57.5 1.0
CG C:ASP57 3.4 58.6 1.0
O G:FGA6 3.5 0.6 1.0
OH C:TYR265 3.7 43.5 1.0
CB C:ASP85 4.0 55.9 1.0
CE1 C:PHE260 4.0 57.5 1.0
O C:HIS241 4.0 67.2 1.0
OD1 C:ASP85 4.2 51.3 1.0
CE1 C:HIS167 4.2 57.6 1.0
OD1 C:ASP57 4.3 56.5 1.0
ND1 C:HIS241 4.3 76.3 1.0
ND1 C:HIS59 4.3 56.5 1.0
CD2 C:HIS118 4.4 46.8 1.0
OD1 C:ASN117 4.4 47.9 1.0
CB C:ASP57 4.4 57.8 1.0
NE2 C:HIS167 4.5 57.1 1.0
CG C:HIS59 4.5 55.2 1.0
CZ C:TYR265 4.5 45.7 1.0
CZ C:PHE260 4.5 56.1 1.0
C G:FGA6 4.5 0.9 1.0
NE2 C:HIS118 4.6 45.2 1.0
ND2 C:ASN117 4.6 38.8 1.0
OXT G:FGA6 4.7 0.6 1.0
C C:HIS241 4.8 66.6 1.0
CE1 C:HIS241 4.8 80.3 1.0
CG C:ASN117 4.9 44.7 1.0
O3 G:1ZN5 5.0 0.1 1.0

Manganese binding site 3 out of 4 in 2nyl

Go back to Manganese Binding Sites List in 2nyl
Manganese binding site 3 out of 4 in the Crystal Structure of Protein Phosphatase 2A (PP2A) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated


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) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mn501

b:52.5
occ:1.00
 OD1 F:ASN117 2.0 44.2 1.0
ND1 F:HIS241 2.1 64.8 1.0
NE2 F:HIS167 2.2 51.9 1.0
OD2 F:ASP85 2.4 56.3 1.0
CE1 F:HIS241 2.5 67.3 1.0
CG F:ASN117 2.6 41.5 1.0
CE1 F:HIS167 2.8 54.0 1.0
ND2 F:ASN117 2.8 33.5 1.0
MN F:MN502 2.9 57.3 1.0
CG F:ASP85 3.1 53.1 1.0
OD1 F:ASP85 3.3 50.6 1.0
CG F:HIS241 3.4 67.1 1.0
CD2 F:HIS167 3.4 55.2 1.0
OD2 F:ASP57 3.6 53.7 1.0
O F:HIS241 3.6 59.4 1.0
NE2 F:HIS241 3.7 65.7 1.0
ND1 F:HIS167 4.0 55.4 1.0
CB F:ASN117 4.1 42.4 1.0
CA F:HIS241 4.2 60.5 1.0
CD2 F:HIS241 4.2 66.6 1.0
CB F:HIS241 4.2 64.6 1.0
CD2 F:HIS118 4.2 48.1 1.0
C F:HIS241 4.4 59.4 1.0
CG F:HIS167 4.4 55.2 1.0
CB F:ASP85 4.4 52.7 1.0
CG F:ASP57 4.5 52.5 1.0
OD1 F:ASP57 4.5 51.6 1.0
N F:ASN117 4.7 43.1 1.0
NE2 F:HIS59 4.7 51.3 1.0
O3 H:1ZN5 4.8 95.8 1.0
O H:FGA6 4.8 94.8 1.0
NE2 F:HIS118 4.8 48.2 1.0
CA F:ASN117 4.9 42.8 1.0

Manganese binding site 4 out of 4 in 2nyl

Go back to Manganese Binding Sites List in 2nyl
Manganese binding site 4 out of 4 in the Crystal Structure of Protein Phosphatase 2A (PP2A) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated


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) Holoenzyme with the Catalytic Subunit Carboxyl Terminus Truncated within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mn502

b:57.3
occ:1.00
 OD2 F:ASP85 1.9 56.3 1.0
OD2 F:ASP57 2.2 53.7 1.0
NE2 F:HIS59 2.3 51.3 1.0
MN F:MN501 2.9 52.5 1.0
CE1 F:HIS59 3.1 49.2 1.0
CG F:ASP85 3.2 53.1 1.0
CD2 F:HIS59 3.4 50.3 1.0
CG F:ASP57 3.5 52.5 1.0
O H:FGA6 3.5 94.8 1.0
OH F:TYR265 3.5 42.0 1.0
O F:HIS241 4.0 59.4 1.0
CB F:ASP85 4.1 52.7 1.0
OD1 F:ASP85 4.1 50.6 1.0
OXT H:FGA6 4.1 97.3 1.0
CD2 F:HIS118 4.2 48.1 1.0
C H:FGA6 4.2 96.5 1.0
OD1 F:ASP57 4.3 51.6 1.0
CE1 F:PHE260 4.3 52.7 1.0
NE2 F:HIS118 4.3 48.2 1.0
ND1 F:HIS59 4.3 48.5 1.0
CZ F:TYR265 4.4 41.0 1.0
OD1 F:ASN117 4.4 44.2 1.0
CE1 F:HIS167 4.4 54.0 1.0
CB F:ASP57 4.4 52.2 1.0
CG F:HIS59 4.5 48.4 1.0
ND2 F:ASN117 4.5 33.5 1.0
ND1 F:HIS241 4.6 64.8 1.0
NE2 F:HIS167 4.6 51.9 1.0
O3 H:1ZN5 4.7 95.8 1.0
CZ F:PHE260 4.7 53.9 1.0
CE1 F:TYR265 4.9 41.9 1.0
CE1 F:HIS241 4.9 67.3 1.0
CG F:ASN117 4.9 41.5 1.0
C F:HIS241 5.0 59.4 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 14:40:53 2024

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