Magnesium in PDB 3pux: Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-BEF3

All present enzymatic activity of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-BEF3:
3.6.3.19;

The structure of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-BEF3, PDB code: 3pux was solved by M.L.Oldham, J.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.81 / 2.30
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	82.130, 97.340, 112.840, 85.58, 78.98, 72.25
R / Rfree (%)	22.8 / 26.5

The structure of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-BEF3 also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Magnesium atom in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-BEF3 (pdb code 3pux). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-BEF3, PDB code: 3pux:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-BEF3


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 An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-BEF3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1501 b:18.5 occ:1.00 O A:HOH382 1.8 21.1 1.0 O2B A:ADP2501 2.0 17.7 1.0 O A:HOH383 2.0 20.7 1.0 OG A:SER43 2.0 19.7 1.0 F1 A:BEF3001 2.1 19.9 1.0 OE1 A:GLN82 2.2 19.3 1.0 PB A:ADP2501 3.2 19.6 1.0 CB A:SER43 3.2 20.0 1.0 CD A:GLN82 3.3 16.0 1.0 BE A:BEF3001 3.3 17.8 1.0 O3B A:ADP2501 3.5 19.8 1.0 NE2 A:GLN82 3.8 12.8 1.0 O1A A:ADP2501 3.8 20.0 1.0 OD2 A:ASP158 3.8 20.8 1.0 OD1 A:ASP158 3.9 19.1 1.0 N A:SER43 3.9 21.2 1.0 O3A A:ADP2501 4.0 18.8 1.0 CA A:SER43 4.1 21.0 1.0 F2 A:BEF3001 4.1 20.4 1.0 PA A:ADP2501 4.3 17.4 1.0 CG A:ASP158 4.3 19.5 1.0 O1B A:ADP2501 4.4 17.7 1.0 OE2 A:GLU159 4.4 24.2 1.0 F3 A:BEF3001 4.5 18.4 1.0 N B:GLY136 4.6 17.2 1.0 O2A A:ADP2501 4.6 21.5 1.0 CG A:GLN82 4.6 16.3 1.0 O A:HOH437 4.8 38.2 1.0 CB A:GLN82 4.9 16.8 1.0 C A:LYS42 5.0 22.3 1.0 CB B:SER135 5.0 19.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-BEF3


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of An Outward-Facing Mbp-Maltose Transporter Complex Bound to Adp-BEF3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1502 b:15.5 occ:1.00 F1 B:BEF3002 1.8 21.4 1.0 O B:HOH382 1.9 33.9 1.0 O B:HOH383 1.9 34.5 1.0 OG B:SER43 2.1 26.6 1.0 OE1 B:GLN82 2.1 23.6 1.0 O2B B:ADP2502 2.3 26.0 1.0 CD B:GLN82 3.1 20.5 1.0 BE B:BEF3002 3.2 22.9 1.0 CB B:SER43 3.3 27.4 1.0 PB B:ADP2502 3.3 26.3 1.0 NE2 B:GLN82 3.4 22.0 1.0 O3B B:ADP2502 3.5 24.6 1.0 O1A B:ADP2502 3.9 24.2 1.0 OE2 B:GLU159 4.0 27.1 1.0 F2 B:BEF3002 4.0 27.0 1.0 OD2 B:ASP158 4.0 22.1 1.0 N B:SER43 4.0 28.5 1.0 OD1 B:ASP158 4.2 24.4 1.0 CA B:SER43 4.2 28.5 1.0 O3A B:ADP2502 4.3 27.8 1.0 F3 B:BEF3002 4.3 21.2 1.0 CG B:GLN82 4.5 20.5 1.0 N A:GLY136 4.5 24.8 1.0 PA B:ADP2502 4.5 29.9 1.0 O1B B:ADP2502 4.5 30.2 1.0 CG B:ASP158 4.6 23.4 1.0 CB A:SER135 4.7 28.1 1.0 CB B:GLN82 4.8 20.7 1.0 CD B:GLU159 4.9 29.2 1.0 O2A B:ADP2502 5.0 29.3 1.0

M.L.Oldham, J.Chen. Snapshots of the Maltose Transporter During Atp Hydrolysis. Proc.Natl.Acad.Sci.Usa V. 108 15152 2011.
ISSN: ISSN 0027-8424
PubMed: 21825153
DOI: 10.1073/PNAS.1108858108