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Open data
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Basic information
Entry | Database: PDB / ID: 2ear | ||||||
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Title | P21 crystal of the SR CA2+-ATPase with bound TG | ||||||
![]() | Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 | ||||||
![]() | HYDROLASE / MEMBRANE PROTEIN / P-TYPE ATPASE / HAD FOLD / Ca2+ / ion pump | ||||||
Function / homology | ![]() positive regulation of cardiac muscle cell contraction / positive regulation of calcium ion import into sarcoplasmic reticulum / H zone / positive regulation of fast-twitch skeletal muscle fiber contraction / positive regulation of ATPase-coupled calcium transmembrane transporter activity / calcium ion import into sarcoplasmic reticulum / negative regulation of striated muscle contraction / regulation of striated muscle contraction / P-type Ca2+ transporter / P-type calcium transporter activity ...positive regulation of cardiac muscle cell contraction / positive regulation of calcium ion import into sarcoplasmic reticulum / H zone / positive regulation of fast-twitch skeletal muscle fiber contraction / positive regulation of ATPase-coupled calcium transmembrane transporter activity / calcium ion import into sarcoplasmic reticulum / negative regulation of striated muscle contraction / regulation of striated muscle contraction / P-type Ca2+ transporter / P-type calcium transporter activity / I band / endoplasmic reticulum-Golgi intermediate compartment / sarcoplasmic reticulum membrane / sarcoplasmic reticulum / intracellular calcium ion homeostasis / calcium ion transport / calcium ion binding / endoplasmic reticulum membrane / perinuclear region of cytoplasm / endoplasmic reticulum / ATP hydrolysis activity / ATP binding / membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Takahashi, M. / Kondou, Y. / Toyoshima, C. | ||||||
![]() | ![]() Title: Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors Authors: Takahashi, M. / Kondou, Y. / Toyoshima, C. #1: ![]() Title: Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution Authors: Toyoshima, C. / Nakasako, M. / Nomura, H. / Ogawa, H. #2: ![]() Title: Structural changes in the calcium pump accompanying the dissociation of calcium Authors: Toyoshima, C. / Nomura, H. #3: ![]() Title: Crystal structure of the calcium pump with a bound ATP analogue Authors: Toyoshima, C. / Mizutani, T. #4: ![]() Title: Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues Authors: Toyoshima, C. / Nomura, H. / Tsuda, T. #5: ![]() Title: Structural role of countertransport revealed in Ca(2+) pump crystal structure in the absence of Ca(2+) Authors: Obara, K. / Miyashita, N. / Xu, C. / Toyoshima, I. / Sugita, Y. / Inesi, G. / Toyoshima, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 199.7 KB | Display | ![]() |
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PDB format | ![]() | 156.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2eatC ![]() 2eauC ![]() 4yclC ![]() 1iwoS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 109628.617 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Chemical | ChemComp-TG1 / |
Sequence details | THE C-TERMINAL RESIDUES IN UNP ENTRY P04191 ARE FROM 994 TO 1001, DPEDERRK. IN ISOFORM SERCA1A, ...THE C-TERMINAL RESIDUES IN UNP ENTRY P04191 ARE FROM 994 TO 1001, DPEDERRK. IN ISOFORM SERCA1A, THERE IS ONLY ONE C-TERMINAL RESIDUE 994 GLY. |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.23 Å3/Da / Density % sol: 70.95 % |
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Crystal grow | Temperature: 283 K / Method: microdialysis / pH: 6.1 / Details: PEG 400, pH 6.1, MICRODIALYSIS, temperature 283K |
-Data collection
Diffraction |
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Radiation |
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Reflection | Resolution: 3.1→20 Å / Num. all: 33292 / Num. obs: 33259 / % possible obs: 99.9 % / Observed criterion σ(F): 5.88 / Observed criterion σ(I): -2 / Redundancy: 6.4 % / Rmerge(I) obs: 0.056 / Net I/σ(I): 27.6 | ||||||||||||||||||
Reflection shell | Resolution: 3.1→3.18 Å / Redundancy: 5.6 % / Rmerge(I) obs: 0.429 / Mean I/σ(I) obs: 2.7 / % possible all: 99.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1IWO Resolution: 3.1→14.95 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 1285345.79 / Data cutoff low absF: 0 / Isotropic thermal model: GROUP / Cross valid method: THROUGHOUT / σ(F): 3 / Stereochemistry target values: maximum likelihood
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 19.2959 Å2 / ksol: 0.196708 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 95.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3.1→14.95 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.1→3.29 Å / Rfactor Rfree error: 0.026 / Total num. of bins used: 6
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Xplor file |
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