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Calcium in PDB 2j82: Structural Analysis of the PP2C Family Phosphatase Tppha From Thermosynechococcus Elongatus

Protein crystallography data

The structure of Structural Analysis of the PP2C Family Phosphatase Tppha From Thermosynechococcus Elongatus, PDB code: 2j82 was solved by C.Schlicker, N.Kloft, K.Forchhammer, S.Becker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 75.81 / 1.28
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 38.216, 151.799, 82.505, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 20.4

Other elements in 2j82:

The structure of Structural Analysis of the PP2C Family Phosphatase Tppha From Thermosynechococcus Elongatus also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structural Analysis of the PP2C Family Phosphatase Tppha From Thermosynechococcus Elongatus (pdb code 2j82). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structural Analysis of the PP2C Family Phosphatase Tppha From Thermosynechococcus Elongatus, PDB code: 2j82:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 2j82

Go back to Calcium Binding Sites List in 2j82
Calcium binding site 1 out of 2 in the Structural Analysis of the PP2C Family Phosphatase Tppha From Thermosynechococcus Elongatus


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structural Analysis of the PP2C Family Phosphatase Tppha From Thermosynechococcus Elongatus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca2241

b:22.6
occ:1.00
O A:HOH2024 2.3 28.4 1.0
O A:HOH2026 2.3 19.5 1.0
O A:GLY1035 2.3 22.7 1.0
OD1 A:ASP1034 2.3 19.6 1.0
O A:HOH2132 2.3 29.6 1.0
O A:HOH2046 2.6 36.2 1.0
CG A:ASP1034 3.5 18.9 1.0
C A:GLY1035 3.5 22.2 1.0
MG A:MG2242 3.6 21.4 0.5
CA A:CA2243 3.6 21.4 0.5
OD2 A:ASP1034 4.0 21.2 1.0
N A:GLY1035 4.1 18.6 1.0
O A:HOH2103 4.2 22.9 1.0
O A:HOH2021 4.2 35.8 1.0
O A:HOH2045 4.2 25.0 1.0
C A:ASP1034 4.3 18.3 1.0
O A:HOH2134 4.3 19.5 1.0
CA A:GLY1035 4.4 19.5 1.0
CB A:GLN1017 4.4 20.9 1.0
OD1 A:ASP1018 4.4 18.5 1.0
OE1 A:GLN1017 4.4 31.9 1.0
N A:MET1036 4.5 28.5 1.0
ND2 A:ASN1232 4.5 17.3 1.0
O A:ASP1034 4.6 18.8 1.0
OD1 A:ASP1231 4.6 23.0 1.0
CB A:ASP1034 4.6 17.0 1.0
O A:HOH2135 4.7 28.6 1.0
CA A:MET1036 4.7 29.9 1.0
CA A:ASP1034 4.8 17.3 1.0
CB A:MET1036 4.8 28.5 1.0

Calcium binding site 2 out of 2 in 2j82

Go back to Calcium Binding Sites List in 2j82
Calcium binding site 2 out of 2 in the Structural Analysis of the PP2C Family Phosphatase Tppha From Thermosynechococcus Elongatus


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structural Analysis of the PP2C Family Phosphatase Tppha From Thermosynechococcus Elongatus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca2243

b:21.4
occ:0.48
MG A:MG2242 0.0 21.4 0.5
O A:HOH2103 1.9 22.9 1.0
O A:HOH2132 2.2 29.6 1.0
OD1 A:ASP1193 2.3 19.0 1.0
OD2 A:ASP1231 2.4 28.6 1.0
OD2 A:ASP1034 2.4 21.2 1.0
O A:HOH2134 2.4 19.5 1.0
CG A:ASP1034 3.1 18.9 1.0
OD1 A:ASP1034 3.1 19.6 1.0
CG A:ASP1193 3.3 19.1 1.0
CG A:ASP1231 3.3 21.8 1.0
OD1 A:ASP1231 3.6 23.0 1.0
CA A:CA2241 3.6 22.6 1.0
O A:HOH2046 3.7 36.2 1.0
OD2 A:ASP1193 3.8 28.8 1.0
O A:HOH2133 4.1 41.4 1.0
O A:HOH2021 4.3 35.8 1.0
O A:HOH2068 4.3 23.2 1.0
O A:HOH2026 4.3 19.5 1.0
N A:GLY1194 4.4 18.2 0.5
O A:HOH2044 4.4 19.2 1.0
CB A:ASP1034 4.5 17.0 1.0
CB A:ASP1193 4.6 20.0 1.0
O A:ASN1232 4.6 18.1 1.0
OD1 A:ASP1018 4.6 18.5 1.0
CB A:ASP1231 4.6 20.5 1.0
N A:ASP1193 4.7 17.9 1.0
C A:ASP1193 4.8 18.7 1.0
CA A:ASP1193 4.9 18.3 1.0

Reference:

C.Schlicker, O.Fokina, N.Kloft, T.Grune, S.Becker, G.M.Sheldrick, K.Forchhammer. Structural Analysis of the PP2C Phosphatase Tppha From Thermosynechococcus Elongatus: A Flexible Flap Subdomain Controls Access to the Catalytic Site. J.Mol.Biol. V. 376 570 2008.
ISSN: ISSN 0022-2836
PubMed: 18164312
DOI: 10.1016/J.JMB.2007.11.097
Page generated: Sat Dec 12 03:41:37 2020

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