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Manganese in PDB 2jft: Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Sulfate

Protein crystallography data

The structure of Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Sulfate, PDB code: 2jft was solved by M.Bellinzoni, A.Wehenkel, W.Shepard, P.M.Alzari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 1.08
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 76.547, 84.402, 33.609, 90.00, 90.00, 90.00
R / Rfree (%) 11.6 / 16

Other elements in 2jft:

The structure of Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Sulfate also contains other interesting chemical elements:

Magnesium (Mg) 5 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Sulfate (pdb code 2jft). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Sulfate, PDB code: 2jft:

Manganese binding site 1 out of 1 in 2jft

Go back to Manganese Binding Sites List in 2jft
Manganese binding site 1 out of 1 in the Crystal Structure of the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Sulfate


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 the Ppm Ser-Thr Phosphatase Mspp From Mycobacterium Smegmatis in Complex with Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn302

b:10.6
occ:0.89
OD1 A:ASP185 2.1 11.4 1.0
OD2 A:ASP223 2.1 11.9 1.0
O A:HOH579 2.2 13.8 1.0
OD2 A:ASP35 2.2 10.9 1.0
O A:HOH568 2.2 11.0 1.0
O A:HOH451 2.3 12.0 1.0
CG A:ASP223 3.1 10.6 1.0
CG A:ASP35 3.1 9.6 1.0
CG A:ASP185 3.1 12.3 1.0
OD1 A:ASP223 3.4 11.3 1.0
OD1 A:ASP35 3.4 10.7 1.0
OD2 A:ASP185 3.5 22.5 1.0
MG A:MG303 3.6 13.2 0.2
MG A:MG301 3.8 10.3 1.0
O A:HOH470 3.9 11.9 1.0
O2 A:SO4306 3.9 16.9 0.9
O A:HOH531 4.2 14.7 1.0
O A:HOH559 4.2 20.1 1.0
O A:HOH524 4.2 11.4 1.0
N A:GLY186 4.3 11.4 1.0
O A:HOH496 4.4 11.0 1.0
CB A:ASP223 4.4 11.9 1.0
OD1 A:ASP22 4.4 11.3 1.0
CB A:ASP35 4.4 10.2 1.0
CB A:ASP185 4.4 12.5 1.0
O A:ASN224 4.5 11.2 1.0
N A:ASP185 4.5 11.2 1.0
C A:ASP185 4.7 11.2 1.0
CA A:ASP185 4.8 11.1 1.0
O A:HOH512 4.8 41.0 1.0
CB A:SER184 4.8 11.0 1.0
CA A:GLY186 5.0 12.2 1.0

Reference:

M.Bellinzoni, A.Wehenkel, W.Shepard, P.M.Alzari. Insights Into the Mechanism of Ppm Ser/Thr Phosphatases From the Atomic Resolution Structures of A Mycobacterial Enzyme Structure V. 15 863 2007.
ISSN: ISSN 0969-2126
PubMed: 17637345
DOI: 10.1016/J.STR.2007.06.002
Page generated: Sat Oct 5 14:34:57 2024

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