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Magnesium in PDB 2bha: E. Coli Aminopeptidase P in Complex with Substrate

Enzymatic activity of E. Coli Aminopeptidase P in Complex with Substrate

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

Protein crystallography data

The structure of E. Coli Aminopeptidase P in Complex with Substrate, PDB code: 2bha 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 (°) 138.223, 138.223, 230.841, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the E. Coli Aminopeptidase P in Complex with Substrate (pdb code 2bha). 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 E. Coli Aminopeptidase P in Complex with Substrate, PDB code: 2bha:

Magnesium binding site 1 out of 1 in 2bha

Go back to Magnesium Binding Sites List in 2bha
Magnesium binding site 1 out of 1 in the E. Coli Aminopeptidase P in Complex with Substrate


Mono view


Stereo pair view

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

b:51.1
occ:1.00
O A:HOH2097 2.2 48.7 1.0
O A:HOH2099 2.2 47.2 1.0
O A:HOH2100 2.2 52.5 1.0
O A:ARG399 3.8 43.2 1.0
OE2 A:GLU396 4.0 44.6 1.0
O A:GLN397 4.2 43.5 1.0
O A:GLU396 4.5 41.3 1.0
O A:HOH2101 4.7 43.0 1.0
C A:GLN397 4.8 43.4 1.0
CD A:GLU396 4.8 45.3 1.0
CA A:GLN397 5.0 42.9 1.0
OE1 A:GLU396 5.0 45.6 1.0
C A:ARG399 5.0 43.1 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: Sun Aug 10 09:59:36 2025

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