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Magnesium in PDB 2bh3: Zn Substituted E. Coli Aminopeptidase P in Complex with Product

Enzymatic activity of Zn Substituted E. Coli Aminopeptidase P in Complex with Product

All present enzymatic activity of Zn Substituted E. Coli Aminopeptidase P in Complex with Product:
3.4.11.9;

Protein crystallography data

The structure of Zn Substituted E. Coli Aminopeptidase P in Complex with Product, PDB code: 2bh3 was solved by S.C.Graham, C.S.Bond, H.C.Freeman, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 60.19 / 2.40
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 138.012, 138.012, 230.734, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 20.1

Other elements in 2bh3:

The structure of Zn Substituted E. Coli Aminopeptidase P in Complex with Product also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Zn Substituted E. Coli Aminopeptidase P in Complex with Product (pdb code 2bh3). 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 Zn Substituted E. Coli Aminopeptidase P in Complex with Product, PDB code: 2bh3:

Magnesium binding site 1 out of 1 in 2bh3

Go back to Magnesium Binding Sites List in 2bh3
Magnesium binding site 1 out of 1 in the Zn Substituted E. Coli Aminopeptidase P in Complex with Product


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Zn Substituted E. Coli Aminopeptidase P in Complex with Product within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1003

b:57.1
occ:1.00
O A:HOH2131 2.2 56.4 1.0
O A:HOH2132 2.2 55.1 1.0
O A:HOH2133 2.2 56.8 1.0
O A:ARG399 3.7 42.6 1.0
OE2 A:GLU396 4.1 46.0 1.0
O A:GLN397 4.3 43.1 1.0
O A:GLU396 4.6 43.4 1.0
O A:HOH2107 4.6 53.5 1.0
O A:HOH2134 4.7 49.7 1.0
O A:HOH2081 4.8 52.7 1.0
C A:GLN397 4.8 42.3 1.0
C A:ARG399 4.9 43.6 1.0
CD A:GLU396 4.9 46.3 1.0

Reference:

S.C.Graham, C.S.Bond, H.C.Freeman, J.M.Guss. Structural and Functional Implications of Metal Ion Selection in Aminopeptidase P, A Metalloprotease with A Dinuclear Metal Center. Biochemistry V. 44 13820 2005.
ISSN: ISSN 0006-2960
PubMed: 16229471
DOI: 10.1021/BI0512849
Page generated: Mon Dec 14 07:16:40 2020

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