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Magnesium in PDB 3sf0: Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D64N Complexed with 5'Amp

Enzymatic activity of Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D64N Complexed with 5'Amp

All present enzymatic activity of Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D64N Complexed with 5'Amp:
3.1.3.2;

Protein crystallography data

The structure of Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D64N Complexed with 5'Amp, PDB code: 3sf0 was solved by H.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.12 / 1.35
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 97.897, 97.897, 107.009, 90.00, 90.00, 120.00
R / Rfree (%) 14.2 / 15.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D64N Complexed with 5'Amp (pdb code 3sf0). 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 Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D64N Complexed with 5'Amp, PDB code: 3sf0:

Magnesium binding site 1 out of 1 in 3sf0

Go back to Magnesium Binding Sites List in 3sf0
Magnesium binding site 1 out of 1 in the Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D64N Complexed with 5'Amp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D64N Complexed with 5'Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg263

b:8.7
occ:1.00
 O3P A:AMP264 2.1 9.8 1.0
O A:HOH332 2.1 8.7 1.0
OD1 A:ASN64 2.1 8.6 1.0
O A:ASP66 2.1 8.8 1.0
OD1 A:ASP181 2.1 8.8 1.0
O A:HOH290 2.2 9.3 1.0
CG A:ASN64 3.1 8.8 1.0
CG A:ASP181 3.1 8.7 1.0
C A:ASP66 3.3 8.4 1.0
P A:AMP264 3.4 9.9 1.0
OD2 A:ASP181 3.4 9.0 1.0
ND2 A:ASN64 3.6 10.4 1.0
O2P A:AMP264 3.7 10.1 1.0
O A:HOH313 4.0 11.0 1.0
CA A:ASP66 4.0 8.9 1.0
N A:ASP66 4.0 8.7 1.0
OD2 A:ASP185 4.0 9.3 1.0
CB A:ASP66 4.1 9.8 1.0
OG1 A:THR68 4.2 8.6 1.0
O1P A:AMP264 4.2 10.2 1.0
OH A:TYR221 4.3 10.4 1.0
CB A:ASN64 4.3 8.1 1.0
N A:GLU67 4.4 8.3 1.0
O5' A:AMP264 4.4 13.2 1.0
CB A:ASP181 4.5 8.6 1.0
CB A:GLU67 4.5 9.0 1.0
C5' A:AMP264 4.7 13.5 1.0
O A:HOH282 4.7 10.6 1.0
CA A:GLU67 4.7 8.6 1.0
N A:THR68 4.7 8.4 1.0
C A:LEU65 4.7 8.1 1.0
C A:GLU67 4.7 8.5 1.0
N A:ASP181 4.8 7.9 1.0
OD1 A:ASP185 4.8 10.4 1.0
CG A:ASP185 4.8 9.5 1.0
CB A:THR68 4.9 8.6 1.0

Reference:

H.Singh, T.J.Reilly, J.J.Tanner. Structural Basis of the Inhibition of Class C Acid Phosphatases By Adenosine 5'-Phosphorothioate. Febs J. V. 278 4374 2011.
ISSN: ISSN 1742-464X
PubMed: 21933344
DOI: 10.1111/J.1742-4658.2011.08360.X
Page generated: Thu Aug 15 10:55:13 2024

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