Magnesium in PDB 3fps: The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic and Adp

All present enzymatic activity of The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic and Adp:
3.6.3.8;

The structure of The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic and Adp, PDB code: 3fps was solved by K.Moncoq, J.P.Morth, M.Bublitz, M.Laursen, P.Nissen, H.S.Young, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.89 / 3.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	62.340, 96.500, 155.130, 90.00, 94.84, 90.00
R / Rfree (%)	22.2 / 24.1

The binding sites of Magnesium atom in the The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic and Adp (pdb code 3fps). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic and Adp, PDB code: 3fps:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic and Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic and Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg995 b:61.9 occ:1.00 O3B A:ADP1002 2.2 0.1 1.0 PB A:ADP1002 2.5 0.1 1.0 O2B A:ADP1002 2.5 0.1 1.0 O1B A:ADP1002 2.9 0.1 1.0 OD1 A:ASP351 3.9 85.4 1.0 O3A A:ADP1002 4.0 0.1 1.0 OG1 A:THR353 4.2 65.8 1.0 O A:HOH1008 4.3 84.5 1.0 CG A:ASP351 4.4 83.3 1.0 CB A:ASP351 4.5 82.3 1.0 O A:THR353 4.7 75.0 1.0 PA A:ADP1002 4.9 0.1 1.0

Magnesium binding site 2 out of 2 in the The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic and Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic and Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg996 b:0.8 occ:1.00 O2 A:CZA1001 1.6 0.2 1.0 OE1 A:GLN56 2.0 0.2 1.0 O1 A:CZA1001 2.5 0.2 1.0 C6 A:CZA1001 2.6 0.2 1.0 CD A:GLN56 3.1 0.8 1.0 C2 A:CZA1001 3.2 0.2 1.0 C3 A:CZA1001 3.3 0.2 1.0 NE2 A:GLN56 3.7 0.5 1.0 C5 A:CZA1001 4.0 0.2 1.0 CG A:GLN56 4.2 0.1 1.0 CB A:GLN56 4.3 0.9 1.0 O A:GLN56 4.5 0.9 1.0 C4 A:CZA1001 4.5 0.2 1.0 C1 A:CZA1001 4.7 0.2 1.0 CA A:GLN56 4.8 0.3 1.0 CG2 A:VAL62 4.9 0.6 1.0 N1 A:CZA1001 4.9 0.2 1.0 OD2 A:ASP59 4.9 0.8 1.0 C7 A:CZA1001 5.0 0.2 1.0

M.Laursen, M.Bublitz, K.Moncoq, C.Olesen, J.V.Moller, H.S.Young, P.Nissen, J.P.Morth. Cyclopiazonic Acid Is Complexed to A Divalent Metal Ion When Bound to the Sarcoplasmic Reticulum CA2+-Atpase. J.Biol.Chem. V. 284 13513 2009.
ISSN: ISSN 0021-9258
PubMed: 19289472
DOI: 10.1074/JBC.C900031200