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Magnesium in PDB 3ocz: Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Complexed with the Inhibitor Adenosine 5-O-Thiomonophosphate

Enzymatic activity of Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Complexed with the Inhibitor Adenosine 5-O-Thiomonophosphate

All present enzymatic activity of Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Complexed with the Inhibitor Adenosine 5-O-Thiomonophosphate:
3.1.3.2;

Protein crystallography data

The structure of Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Complexed with the Inhibitor Adenosine 5-O-Thiomonophosphate, PDB code: 3ocz was solved by H.Singh, J.Schuermann, T.Reilly, M.Calcutt, J.Tanner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.29 / 1.35
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 98.179, 98.179, 107.020, 90.00, 90.00, 120.00
R / Rfree (%) 13.8 / 15.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Complexed with the Inhibitor Adenosine 5-O-Thiomonophosphate (pdb code 3ocz). 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 Complexed with the Inhibitor Adenosine 5-O-Thiomonophosphate, PDB code: 3ocz:

Magnesium binding site 1 out of 1 in 3ocz

Go back to Magnesium Binding Sites List in 3ocz
Magnesium binding site 1 out of 1 in the Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Complexed with the Inhibitor Adenosine 5-O-Thiomonophosphate


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 Complexed with the Inhibitor Adenosine 5-O-Thiomonophosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg263

b:7.4
occ:1.00
 OP1 A:SRA264 2.0 10.1 1.0
OD2 A:ASP64 2.1 7.8 1.0
O A:HOH485 2.1 7.4 1.0
O A:ASP66 2.1 7.0 1.0
OD1 A:ASP181 2.1 7.3 1.0
O A:HOH484 2.2 7.9 1.0
CG A:ASP64 3.0 7.8 1.0
CG A:ASP181 3.1 7.0 1.0
C A:ASP66 3.3 6.7 1.0
OD1 A:ASP64 3.4 8.7 1.0
OD2 A:ASP181 3.5 7.4 1.0
P A:SRA264 3.5 10.4 1.0
CA A:ASP66 4.0 7.1 1.0
OD2 A:ASP185 4.0 7.4 1.0
OG1 A:THR68 4.1 8.1 1.0
CB A:ASP66 4.1 7.8 1.0
N A:ASP66 4.1 7.2 1.0
O A:HOH483 4.1 10.6 1.0
S2P A:SRA264 4.3 10.9 1.0
CB A:ASP64 4.3 7.0 1.0
OP3 A:SRA264 4.3 9.8 1.0
OH A:TYR221 4.4 8.8 1.0
N A:GLU67 4.4 6.7 1.0
CB A:ASP181 4.5 7.1 1.0
O5' A:SRA264 4.5 10.8 1.0
CB A:GLU67 4.5 7.5 1.0
C5' A:SRA264 4.7 10.6 1.0
N A:ASP181 4.7 6.5 1.0
CA A:GLU67 4.7 6.7 1.0
O A:HOH472 4.7 8.5 1.0
C A:GLU67 4.8 6.3 1.0
N A:THR68 4.8 6.7 1.0
OD1 A:ASP185 4.8 8.4 1.0
C A:LEU65 4.8 7.0 1.0
CG A:ASP185 4.8 7.3 1.0
CB A:THR68 5.0 7.4 1.0
CB A:ASN182 5.0 7.1 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: Mon Aug 11 01:08:07 2025

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