› 5a3q

X-ray diffraction
3.05Å resolution

Crystal structure of the (SR) Calcium ATPase E2-vanadate complex bound to thapsigargin and TNP-AMPPCP

Released:
DOI: 10.2210/pdb5a3q/pdb
PDB entry 5a3q coloured by chain, front view.
PDB entry 5a3q coloured by chain, side view.
PDB entry 5a3q coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Crystal Structure of the Vanadate-Inhibited Ca(2+)-ATPase.
Clausen JD, Bublitz M, Arnou B, Olesen C, Andersen JP, Møller JV, Nissen P
Structure 24 617-623 (2016)
PMID: 27050689

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O + Ca(2+)(Side 1) = ADP + phosphate + Ca(2+)(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137501 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 Chain: A
Molecule details ›
Chain: A
Length: 995 amino acids
Theoretical weight: 109.63 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P04191 (Residues: 1-993; Coverage: 99%)
  • Best match: P04191-2 (Residues: 1-994)
Gene name: ATP2A1
Sequence domains:
Structure domains:

Ligands and Environments

6 bound ligands:
Ligand TG1 1 x TG1
Ligand VN4 1 x VN4
Ligand DL5 1 x DL5
Ligand MG 2 x MG
Ligand K 1 x K
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)
Spacegroup: P21212
Unit cell:
a: 86.427Å b: 118.781Å c: 141.828Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.2 0.258

Quick links

Citations

4 review citations

Linking Biochemical and Structural States of SERCA: Achievements, Challenges, and New Opportunities.
Aguayo-Ortiz et al. (2020)
3 more

4 mentions without citation

Interaction of Vanadium Complexes with Proteins: Revisiting the Reported Structures in the Protein Data Bank (PDB) since 2015.
Santos et al. (2023)
3 more