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Magnesium in PDB 4ijx: Crystal Structure of Human AP4A Hydrolase E58A Mutant Complexed with Dpo

Enzymatic activity of Crystal Structure of Human AP4A Hydrolase E58A Mutant Complexed with Dpo

All present enzymatic activity of Crystal Structure of Human AP4A Hydrolase E58A Mutant Complexed with Dpo:
3.6.1.17;

Protein crystallography data

The structure of Crystal Structure of Human AP4A Hydrolase E58A Mutant Complexed with Dpo, PDB code: 4ijx was solved by H.Ge, X.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.10
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 72.369, 72.369, 133.379, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 23.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human AP4A Hydrolase E58A Mutant Complexed with Dpo (pdb code 4ijx). 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 Human AP4A Hydrolase E58A Mutant Complexed with Dpo, PDB code: 4ijx:

Magnesium binding site 1 out of 1 in 4ijx

Go back to Magnesium Binding Sites List in 4ijx
Magnesium binding site 1 out of 1 in the Crystal Structure of Human AP4A Hydrolase E58A Mutant Complexed with Dpo


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 Human AP4A Hydrolase E58A Mutant Complexed with Dpo within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:26.7
occ:1.00
CB A:GLU53 3.3 32.4 1.0
CG A:GLU53 3.4 41.7 1.0
N A:ASP50 3.6 31.6 1.0
CB A:ASP50 3.8 31.3 1.0
CG A:GLU49 4.1 39.2 1.0
CA A:GLU49 4.3 35.8 1.0
CA A:ASP50 4.4 31.4 1.0
C A:GLU49 4.5 32.1 1.0
CD A:GLU53 4.6 48.8 1.0
O A:GLY48 4.8 39.9 1.0
CB A:GLU49 4.8 36.9 1.0
CA A:GLU53 4.8 26.5 1.0
O A:ASP50 4.9 28.4 1.0

Reference:

H.Ge, X.Chen, W.Yang, L.Niu, M.Teng. Crystal Structure of Wild-Type and Mutant Human AP4A Hydrolase. Biochem.Biophys.Res.Commun. V. 432 16 2013.
ISSN: ISSN 0006-291X
PubMed: 23384440
DOI: 10.1016/J.BBRC.2013.01.095
Page generated: Fri Aug 16 16:45:37 2024

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