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Potassium in PDB 3fpb: The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic Acid with Atp

Enzymatic activity of The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic Acid with Atp

All present enzymatic activity of The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic Acid with Atp:
3.6.3.8;

Protein crystallography data

The structure of The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic Acid with Atp, PDB code: 3fpb 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) 24.94 / 2.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 175.360, 69.870, 143.500, 90.00, 107.16, 90.00
R / Rfree (%) 18.3 / 23.1

Other elements in 3fpb:

The structure of The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic Acid with Atp also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Magnesium (Mg) 3 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic Acid with Atp (pdb code 3fpb). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic Acid with Atp, PDB code: 3fpb:

Potassium binding site 1 out of 1 in 3fpb

Go back to Potassium Binding Sites List in 3fpb
Potassium binding site 1 out of 1 in the The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic Acid with Atp


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of The Structure of Sarcoplasmic Reticulum CA2+-Atpase Bound to Cyclopiazonic Acid with Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K997

b:0.7
occ:1.00
 O A:HOH1068 2.5 58.3 1.0
O A:ALA714 2.8 58.5 1.0
O A:LYS712 2.9 62.7 1.0
O A:LEU711 3.0 52.8 1.0
OE2 A:GLU732 3.1 70.1 1.0
C A:LYS712 3.6 55.7 1.0
OE1 A:GLU732 3.6 72.8 1.0
CD A:GLU732 3.7 69.3 1.0
C A:ALA714 3.8 61.2 1.0
CA A:LYS712 3.9 54.3 1.0
O A:GLU715 3.9 58.8 1.0
N A:GLY717 4.0 52.3 1.0
C A:LEU711 4.0 47.4 1.0
NZ A:LYS712 4.1 70.8 1.0
C A:GLU715 4.2 55.5 1.0
CA A:ILE716 4.3 44.2 1.0
N A:ALA714 4.3 47.4 1.0
N A:ILE716 4.4 52.2 1.0
C A:ILE716 4.4 55.8 1.0
N A:LYS712 4.4 46.2 1.0
N A:LYS713 4.5 54.0 1.0
CA A:ALA714 4.6 46.7 1.0
C A:LYS713 4.6 52.8 1.0
N A:GLU715 4.7 62.5 1.0
CD A:LYS712 4.7 0.6 1.0
CA A:GLU715 4.8 60.0 1.0
CE A:LYS712 4.8 0.3 1.0
CA A:GLY717 4.8 41.0 1.0
O A:ALA730 4.9 67.4 1.0
CB A:ALA714 4.9 43.9 1.0

Reference:

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
Page generated: Sat Aug 9 04:56:46 2025

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