Magnesium in PDB 3fp2: Crystal Structure of TOM71 Complexed with HSP82 C-Terminal Fragment

The structure of Crystal Structure of TOM71 Complexed with HSP82 C-Terminal Fragment, PDB code: 3fp2 was solved by J.Li, X.Qian, J.Hu, B.Sha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.99 / 1.98
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.863, 116.288, 150.743, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 23.6

The structure of Crystal Structure of TOM71 Complexed with HSP82 C-Terminal Fragment also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of TOM71 Complexed with HSP82 C-Terminal Fragment (pdb code 3fp2). 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 TOM71 Complexed with HSP82 C-Terminal Fragment, PDB code: 3fp2:

Magnesium binding site 1 out of 1 in the Crystal Structure of TOM71 Complexed with HSP82 C-Terminal Fragment


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 TOM71 Complexed with HSP82 C-Terminal Fragment within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg640 b:51.8 occ:1.00 O A:HOH46 3.1 35.7 1.0 OG A:SER265 3.2 32.9 1.0 OG A:SER563 3.3 33.5 1.0 OG A:SER268 3.7 29.9 0.5 CB A:SER563 3.9 34.2 1.0 CB A:SER265 3.9 29.8 1.0 OE1 A:GLN565 3.9 48.9 1.0 O A:HOH35 4.3 34.1 1.0 CB A:THR267 4.3 29.8 1.0 CB A:GLN565 4.4 38.7 1.0 CA A:SER563 4.5 34.5 1.0 CG2 A:THR267 4.7 29.5 1.0 CD1 A:ILE520 4.8 28.8 1.0 N A:SER268 4.8 29.5 0.5 N A:SER268 4.8 29.6 0.5 CG1 A:ILE520 4.9 29.3 1.0 CD A:GLN565 4.9 44.9 1.0 CB A:SER268 5.0 29.2 0.5

J.Li, X.Qian, J.Hu, B.Sha. Molecular Chaperone HSP70/HSP90 Prepares the Mitochondrial Outer Membrane Translocon Receptor TOM71 For Preprotein Loading. J.Biol.Chem. V. 284 23852 2009.
ISSN: ISSN 0021-9258
PubMed: 19581297
DOI: 10.1074/JBC.M109.023986