Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
ATP Adenosine-5'-triphosphate
CZA (6ar,11as,11br)-10-acetyl-9-hydroxy-7,7-dimethyl-2,6,6a,7,11a,11b-hexahydro-11h-pyrrolo[1',2':2,3]isoindolo[4,5,6-Cd]indol-11-one
K Potassium ion
MF4 Tetrafluoromagnesate(2-)
MG Magnesium ion
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 3FPB   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : The Structure of Sarcoplasmic Reticulum Ca2+-ATPase Bound To Cyclopiazonic acid with ATP
Release Data : 2009-04-07
Compound :
mol_id molecule chains synonym
1 Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 A SERCA1, Calcium pump 1, Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform, SR Ca(2+)-ATPase 1, Endoplasmic reticulum class 1/2 Ca(2+) ATPase
ec: 3.6.3.8
Source :
mol_id organism_scientific organism_common
1 Oryctolagus cuniculus  (taxid:9986) Rabbit
tissue: twitch skeletal muscle
Authors : Moncoq, K., Morth, J.P., Bublitz, M., Laursen, M., Nissen, P., Young, H.S.
Keywords : CALCIUM PUMP, SERCA, NONHYDROLYZABLE ATP ANALOG, P-TYPE ATPase, CYCLOPIAZONIC ACID, ION TRANSPORT, PHOSPHOPROTEIN, SARCOPLASMIC RETICULUM, TRANSMEMBRANE, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 2.550 Å )
Citation :

Cyclopiazonic acid is complexed to a divalent metal ion when bound to the sarcoplasmic reticulum Ca2+-ATPase.

Laursen, M.,Bublitz, M.,Moncoq, K.  et al.
(2009)  J.Biol.Chem.  284 : 13513 - 13518

PubMed: 19289472
DOI: 10.1074/jbc.C900031200

Chain : A
UniProt : P04191 (AT2A1_RABIT)
Reaction: EC: Evidence:
Physiological Direction:
ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate 7.2.2.10 PubMed:10914677, PubMed:11438520, PubMed:15189864, PubMed:18075584, PubMed:23996003, PubMed:29081402, PubMed:8117720
left-to-right PubMed:10914677