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Magnesium in PDB 3q44: X-Ray Crystal Structure of Pfa-M1 Bound to Bestatin Derivative 16

Protein crystallography data

The structure of X-Ray Crystal Structure of Pfa-M1 Bound to Bestatin Derivative 16, PDB code: 3q44 was solved by S.Mcgowan, D.C.Greenbaum, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 63.72 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 75.610, 108.591, 118.347, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 22.7

Other elements in 3q44:

The structure of X-Ray Crystal Structure of Pfa-M1 Bound to Bestatin Derivative 16 also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the X-Ray Crystal Structure of Pfa-M1 Bound to Bestatin Derivative 16 (pdb code 3q44). 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 X-Ray Crystal Structure of Pfa-M1 Bound to Bestatin Derivative 16, PDB code: 3q44:

Magnesium binding site 1 out of 1 in 3q44

Go back to Magnesium Binding Sites List in 3q44
Magnesium binding site 1 out of 1 in the X-Ray Crystal Structure of Pfa-M1 Bound to Bestatin Derivative 16


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of X-Ray Crystal Structure of Pfa-M1 Bound to Bestatin Derivative 16 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg9

b:33.4
occ:1.00
O A:HOH1909 2.0 31.0 1.0
O A:HOH1907 2.1 20.5 1.0
O A:HOH1910 2.1 25.6 1.0
O A:HOH1911 2.2 21.2 1.0
O A:HOH1908 2.3 21.4 1.0
OE2 A:GLU957 3.7 20.6 1.0
O A:HOH1682 4.0 24.8 1.0
O A:HOH1912 4.1 32.7 1.0
O A:HOH1902 4.1 20.6 1.0
ND2 A:ASN992 4.1 19.9 1.0
OD2 A:ASP995 4.2 16.5 1.0
CD A:GLU957 4.5 23.1 1.0
O A:HOH1325 4.5 21.4 1.0
O A:HOH1563 4.6 33.4 1.0
O A:HOH6 4.7 16.3 1.0
CG A:GLU957 4.7 21.4 1.0
CE A:LYS311 5.0 19.9 1.0

Reference:

G.Velmourougane, M.B.Harbut, S.Dalal, S.Mcgowan, C.A.Oellig, N.Meinhardt, J.C.Whisstock, M.Klemba, D.C.Greenbaum. Synthesis of New (-)-Bestatin-Based Inhibitor Libraries Reveals A Novel Binding Mode in the S1 Pocket of the Essential Malaria M1 Metalloaminopeptidase. J.Med.Chem. V. 54 1655 2011.
ISSN: ISSN 0022-2623
PubMed: 21366301
DOI: 10.1021/JM101227T
Page generated: Thu Aug 15 09:54:00 2024

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