Magnesium in PDB 3qfu: Crystal Structure of Yeast HSP70 (Bip/KAR2) Complexed with Adp

The structure of Crystal Structure of Yeast HSP70 (Bip/KAR2) Complexed with Adp, PDB code: 3qfu was solved by M.Yan, J.Z.Li, B.D.Sha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.49 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.367, 85.667, 94.921, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 23.8

The binding sites of Magnesium atom in the Crystal Structure of Yeast HSP70 (Bip/KAR2) Complexed with Adp (pdb code 3qfu). 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 Yeast HSP70 (Bip/KAR2) Complexed with Adp, PDB code: 3qfu:

Magnesium binding site 1 out of 1 in the Crystal Structure of Yeast HSP70 (Bip/KAR2) Complexed with Adp


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 Yeast HSP70 (Bip/KAR2) Complexed with Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1 b:18.5 occ:1.00 O1 A:PO4502 2.1 18.0 1.0 O A:HOH581 2.1 15.7 1.0 O3B A:ADP501 2.1 18.2 0.9 O A:HOH583 2.1 17.8 1.0 O A:HOH580 2.2 20.5 1.0 O A:HOH582 2.2 20.4 1.0 P A:PO4502 3.3 18.6 1.0 PB A:ADP501 3.4 18.4 1.0 O3 A:PO4502 3.5 17.8 1.0 O2B A:ADP501 3.7 18.5 1.0 O A:HOH21 3.8 20.3 1.0 O2A A:ADP501 4.0 16.7 1.0 O4 A:PO4502 4.0 18.2 1.0 O A:HOH15 4.0 24.4 1.0 O A:HOH633 4.1 33.1 1.0 OD1 A:ASP244 4.2 21.1 1.0 OE1 A:GLU221 4.2 18.5 1.0 OD2 A:ASP56 4.3 18.2 1.0 O A:HOH588 4.3 27.0 1.0 O3A A:ADP501 4.4 17.3 1.0 O1B A:ADP501 4.4 18.2 1.0 OD2 A:ASP244 4.4 22.3 1.0 O2 A:PO4502 4.4 18.7 1.0 OD1 A:ASP56 4.5 17.6 1.0 CG A:ASP244 4.7 21.6 1.0 CD A:GLU221 4.8 18.1 1.0 PA A:ADP501 4.8 17.4 1.0 CG A:ASP56 4.8 17.2 1.0 CA A:GLY58 5.0 17.7 1.0 O A:HOH12 5.0 21.1 1.0

M.Yan, J.Li, B.Sha. Structural Analysis of the SIL1-Bip Complex Reveals the Mechanism For SIL1 to Function As A Nucleotide-Exchange Factor. Biochem.J. V. 438 447 2011.
ISSN: ISSN 0264-6021
PubMed: 21675960
DOI: 10.1042/BJ20110500