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Magnesium in PDB 3ocx: Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed with 2'-Amp

Enzymatic activity of Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed with 2'-Amp

All present enzymatic activity of Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed with 2'-Amp:
3.1.3.2;

Protein crystallography data

The structure of Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed with 2'-Amp, PDB code: 3ocx 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) 45.42 / 1.90
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 97.870, 97.870, 107.598, 90.00, 90.00, 120.00
R / Rfree (%) 17.8 / 21.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed with 2'-Amp (pdb code 3ocx). 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 D66N Complexed with 2'-Amp, PDB code: 3ocx:

Magnesium binding site 1 out of 1 in 3ocx

Go back to Magnesium Binding Sites List in 3ocx
Magnesium binding site 1 out of 1 in the Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed with 2'-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 D66N Complexed with 2'-Amp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg264

b:15.8
occ:1.00
 O3P A:2AM263 2.2 17.3 1.0
OD2 A:ASP64 2.2 15.5 1.0
O A:HOH372 2.2 18.7 1.0
O A:HOH369 2.2 15.3 1.0
O A:ASN66 2.3 15.5 1.0
OD1 A:ASP181 2.3 12.5 1.0
CG A:ASP64 3.1 17.4 1.0
CG A:ASP181 3.3 20.4 1.0
C A:ASN66 3.4 13.6 1.0
OD1 A:ASP64 3.5 16.6 1.0
OD2 A:ASP181 3.5 16.5 1.0
P A:2AM263 3.6 23.1 1.0
CA A:ASN66 4.0 11.6 1.0
CB A:ASN66 4.0 13.6 1.0
O A:HOH371 4.0 21.9 1.0
O2P A:2AM263 4.0 24.1 1.0
N A:ASN66 4.1 13.3 1.0
OD2 A:ASP185 4.1 14.9 1.0
OG1 A:THR68 4.2 15.4 1.0
O A:HOH373 4.2 32.4 1.0
OH A:TYR221 4.2 21.1 1.0
O A:HOH358 4.3 15.8 1.0
CB A:ASP64 4.3 15.1 1.0
O2' A:2AM263 4.4 23.7 1.0
O1P A:2AM263 4.4 20.5 1.0
N A:GLU67 4.5 17.2 1.0
CB A:ASP181 4.6 12.9 1.0
CB A:GLU67 4.6 13.9 1.0
C A:LEU65 4.8 16.0 1.0
N A:ASP181 4.8 14.7 1.0
N A:THR68 4.9 13.5 1.0
CA A:GLU67 4.9 16.0 1.0
C A:GLU67 4.9 16.3 1.0
CB A:ASN182 4.9 18.2 1.0
OD1 A:ASP185 4.9 18.3 1.0
CG A:ASP185 5.0 20.4 1.0

Reference:

H.Singh, J.P.Schuermann, T.J.Reilly, M.J.Calcutt, J.J.Tanner. Recognition of Nucleoside Monophosphate Substrates By Haemophilus Influenzae Class C Acid Phosphatase. J.Mol.Biol. V. 404 639 2010.
ISSN: ISSN 0022-2836
PubMed: 20934434
DOI: 10.1016/J.JMB.2010.09.065
Page generated: Mon Aug 11 01:08:03 2025

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