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Chlorine in PDB 2pk0: Structure of the S. Agalactiae Serine/Threonine Phosphatase at 2.65 Resolution

Enzymatic activity of Structure of the S. Agalactiae Serine/Threonine Phosphatase at 2.65 Resolution

All present enzymatic activity of Structure of the S. Agalactiae Serine/Threonine Phosphatase at 2.65 Resolution:
3.1.3.16;

Protein crystallography data

The structure of Structure of the S. Agalactiae Serine/Threonine Phosphatase at 2.65 Resolution, PDB code: 2pk0 was solved by M.K.Rantanen, L.Lehtio, L.Rajagopal, C.E.Rubens, A.Goldman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.65 / 2.65
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 139.400, 92.100, 86.900, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 27.1

Other elements in 2pk0:

The structure of Structure of the S. Agalactiae Serine/Threonine Phosphatase at 2.65 Resolution also contains other interesting chemical elements:

Magnesium (Mg) 10 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the S. Agalactiae Serine/Threonine Phosphatase at 2.65 Resolution (pdb code 2pk0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of the S. Agalactiae Serine/Threonine Phosphatase at 2.65 Resolution, PDB code: 2pk0:

Chlorine binding site 1 out of 1 in 2pk0

Go back to Chlorine Binding Sites List in 2pk0
Chlorine binding site 1 out of 1 in the Structure of the S. Agalactiae Serine/Threonine Phosphatase at 2.65 Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the S. Agalactiae Serine/Threonine Phosphatase at 2.65 Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl701

b:67.4
occ:1.00
NE2 D:HIS179 3.0 43.0 1.0
CE1 D:HIS179 3.7 43.2 1.0
CA C:GLY146 4.0 47.8 1.0
CD2 D:HIS179 4.2 44.8 1.0
N C:GLY146 4.4 46.5 1.0
O C:VAL143 4.7 47.2 1.0
O C:LYS144 4.8 51.6 1.0
CD2 D:LEU132 4.8 39.8 1.0
CB D:HIS130 4.9 50.7 1.0
ND1 D:HIS130 4.9 56.0 1.0
ND1 D:HIS179 4.9 44.4 1.0
CG D:HIS130 5.0 54.6 1.0

Reference:

M.K.Rantanen, L.Lehtio, L.Rajagopal, C.E.Rubens, A.Goldman. Structure of Streptococcus Agalactiae Serine/Threonine Phosphatase. the Subdomain Conformation Is Coupled to the Binding of A Third Metal Ion Febs J. V. 274 3128 2007.
ISSN: ISSN 1742-464X
PubMed: 17521332
DOI: 10.1111/J.1742-4658.2007.05845.X
Page generated: Thu Jul 10 23:52:24 2025

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