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Magnesium in PDB 3ocu: Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed with Nmn

Enzymatic activity of Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed with Nmn

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

Protein crystallography data

The structure of Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed with Nmn, PDB code: 3ocu 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) 32.00 / 1.35
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 97.758, 97.758, 106.432, 90.00, 90.00, 120.00
R / Rfree (%) 13.5 / 15.4

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 1 in 3ocu

Go back to Magnesium Binding Sites List in 3ocu
Magnesium binding site 1 out of 1 in the Structure of Recombinant Haemophilus Influenzae E(P4) Acid Phosphatase Mutant D66N Complexed with Nmn


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 Nmn within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg263

b:7.7
occ:1.00
 O3P A:NMN2003 1.9 8.7 1.0
OD2 A:ASP64 2.0 7.8 1.0
O A:HOH435 2.1 8.1 1.0
OD1 A:ASP181 2.1 8.0 1.0
O A:ASN66 2.1 8.7 1.0
O A:HOH434 2.2 8.4 1.0
CG A:ASP64 3.0 8.0 1.0
CG A:ASP181 3.2 7.7 1.0
OD1 A:ASP64 3.3 8.5 1.0
C A:ASN66 3.3 8.2 1.0
P A:NMN2003 3.4 9.1 1.0
OD2 A:ASP181 3.5 8.0 1.0
CA A:ASN66 3.9 8.4 1.0
N A:ASN66 3.9 7.9 1.0
O A:HOH433 4.0 10.0 1.0
OG1 A:THR68 4.0 7.9 1.0
OD2 A:ASP185 4.0 8.3 1.0
CB A:ASN66 4.1 8.3 1.0
O1P A:NMN2003 4.1 8.7 1.0
O2P A:NMN2003 4.2 8.8 1.0
CB A:ASP64 4.3 7.5 1.0
OH A:TYR221 4.4 9.4 1.0
N A:GLU67 4.4 7.8 1.0
O A:HOH469 4.4 12.0 1.0
CB A:ASP181 4.5 8.2 1.0
O5R A:NMN2003 4.5 8.6 1.0
C5R A:NMN2003 4.5 10.1 1.0
CB A:GLU67 4.6 8.4 1.0
C A:LEU65 4.6 7.8 1.0
N A:ASP181 4.7 7.2 1.0
N A:THR68 4.7 7.4 1.0
CA A:GLU67 4.8 7.4 1.0
C A:GLU67 4.8 7.5 1.0
OD1 A:ASP185 4.8 8.9 1.0
CG A:ASP185 4.8 8.4 1.0
CB A:THR68 4.9 8.2 1.0
CB A:ASN182 5.0 8.2 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: Thu Aug 15 08:15:17 2024

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