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Magnesium in PDB 3p96: Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium, Native Form

Enzymatic activity of Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium, Native Form

All present enzymatic activity of Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium, Native Form:
3.1.3.3;

Protein crystallography data

The structure of Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium, Native Form, PDB code: 3p96 was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.97 / 2.05
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 65.530, 109.190, 134.320, 90.00, 90.00, 90.00
R / Rfree (%) 22.9 / 28.1

Other elements in 3p96:

The structure of Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium, Native Form also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium, Native Form (pdb code 3p96). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium, Native Form, PDB code: 3p96:

Magnesium binding site 1 out of 1 in 3p96

Go back to Magnesium Binding Sites List in 3p96
Magnesium binding site 1 out of 1 in the Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium, Native Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium, Native Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg412

b:29.2
occ:1.00
 O A:HOH429 2.1 2.0 1.0
OD2 A:ASP187 2.1 39.4 1.0
O A:ASP189 2.1 36.9 1.0
OD1 A:ASP343 2.2 39.0 1.0
O A:HOH451 2.2 7.6 1.0
O A:HOH440 2.2 15.5 1.0
CG A:ASP187 3.1 38.3 1.0
CG A:ASP343 3.1 39.4 1.0
C A:ASP189 3.3 38.4 1.0
OD1 A:ASP187 3.4 36.9 1.0
OD2 A:ASP343 3.4 39.4 1.0
CA A:ASP189 4.0 38.9 1.0
CB A:ASP189 4.1 40.1 1.0
O A:HOH502 4.1 15.7 1.0
OE2 A:GLU196 4.1 48.3 1.0
N A:ASP189 4.2 37.7 1.0
OG1 A:THR191 4.2 37.5 1.0
OD2 A:ASP347 4.2 37.2 1.0
N A:SER190 4.4 38.9 1.0
CB A:ASP187 4.4 36.2 1.0
CB A:ASP343 4.5 39.4 1.0
N A:ASP343 4.6 37.3 1.0
SD A:MET219 4.6 53.3 1.0
N A:GLY344 4.6 42.0 1.0
CB A:SER190 4.7 41.6 1.0
O A:HOH461 4.8 16.8 1.0
N A:THR191 4.8 38.0 1.0
CA A:SER190 4.8 40.0 1.0
CL A:CL413 4.9 42.9 1.0
C A:VAL188 4.9 35.5 1.0
CA A:ASP343 4.9 39.2 1.0
C A:SER190 4.9 38.4 1.0
CB A:THR191 5.0 35.9 1.0

Reference:

J.Abendroth, A.S.Gardberg, J.I.Robinson, J.S.Christensen, B.L.Staker, P.J.Myler, L.J.Stewart, T.E.Edwards. Sad Phasing Using Iodide Ions in A High-Throughput Structural Genomics Environment. J.Struct.Funct.Genom. V. 12 83 2011.
ISSN: ISSN 1345-711X
PubMed: 21359836
DOI: 10.1007/S10969-011-9101-7
Page generated: Mon Aug 11 01:47:05 2025

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