[English] 日本語
![](img/lk-miru.gif)
- PDB-1deg: THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1deg | ||||||
---|---|---|---|---|---|---|---|
Title | THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE | ||||||
![]() | CALMODULIN | ||||||
![]() | CALCIUM-BINDING PROTEIN | ||||||
Function / homology | ![]() regulation of store-operated calcium channel activity / regulation of high voltage-gated calcium channel activity / : / regulation of response to tumor cell / positive regulation of autophagic cell death / DAPK1-calmodulin complex / : / establishment of protein localization to mitochondrial membrane / type 3 metabotropic glutamate receptor binding / establishment of protein localization to membrane ...regulation of store-operated calcium channel activity / regulation of high voltage-gated calcium channel activity / : / regulation of response to tumor cell / positive regulation of autophagic cell death / DAPK1-calmodulin complex / : / establishment of protein localization to mitochondrial membrane / type 3 metabotropic glutamate receptor binding / establishment of protein localization to membrane / regulation of synaptic vesicle endocytosis / negative regulation of high voltage-gated calcium channel activity / positive regulation of cyclic-nucleotide phosphodiesterase activity / organelle localization by membrane tethering / negative regulation of calcium ion export across plasma membrane / regulation of synaptic vesicle exocytosis / regulation of cardiac muscle cell action potential / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / nitric-oxide synthase binding / positive regulation of ryanodine-sensitive calcium-release channel activity / protein phosphatase activator activity / positive regulation of phosphoprotein phosphatase activity / adenylate cyclase binding / catalytic complex / calcium channel regulator activity / detection of calcium ion / regulation of cardiac muscle contraction / negative regulation of ryanodine-sensitive calcium-release channel activity / calcium channel inhibitor activity / positive regulation of DNA binding / phosphatidylinositol 3-kinase binding / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / enzyme regulator activity / positive regulation of protein dephosphorylation / regulation of calcium-mediated signaling / regulation of ryanodine-sensitive calcium-release channel activity / titin binding / potassium ion transmembrane transport / voltage-gated potassium channel complex / calcium channel complex / response to amphetamine / activation of adenylate cyclase activity / adenylate cyclase activator activity / nitric-oxide synthase regulator activity / regulation of heart rate / sarcomere / regulation of cytokinesis / positive regulation of nitric-oxide synthase activity / calcium-mediated signaling / spindle microtubule / spindle pole / response to calcium ion / G2/M transition of mitotic cell cycle / calcium-dependent protein binding / disordered domain specific binding / myelin sheath / growth cone / vesicle / transmembrane transporter binding / protein autophosphorylation / neuron projection / positive regulation of apoptotic process / protein domain specific binding / centrosome / calcium ion binding / protein kinase binding / protein-containing complex / mitochondrion / nucleoplasm / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Raghunathan, S. / Chandross, R. / Cheng, B.P. / Persechini, A. / Sobottk, S.E. / Kretsinger, R.H. | ||||||
![]() | ![]() Title: The linker of des-Glu84-calmodulin is bent. Authors: Raghunathan, S. / Chandross, R.J. / Cheng, B.P. / Persechini, A. / Sobottka, S.E. / Kretsinger, R.H. #1: ![]() Title: Small-Angle X-Ray Scattering Studies of Calmodulin Mutants with Deletions in the Linker Region of the Central Helix Indicate that the Linker Region Retains a Predominantly A-Helical Conformation Authors: Kataoka, M. / Head, J.F. / Persechini, A. / Kretsinger, R.H. / Engelman, D.M. #2: ![]() Title: Calmodulins with Deletions in the Central Helix Functionally Replace the Native Protein in Yeast Cells Authors: Persechini, A. / Kretsinger, R.H. / Davis, T.N. #3: ![]() Title: The Effects of Deletions in the Central Helix of Calmodulin on Enzyme Activation and Peptide Binding Authors: Persechini, A. / Blumenthal, D.K. / Jarrett, H.W. / Klee, C.B. / Hardy, D.O. / Kretsinger, R.H. #4: ![]() Title: The Central Helix of Calmodulin Functions as a Flexible Tether Authors: Persechini, A. / Kretsinger, R.H. #5: ![]() Title: Toward a Model of the Calmodulin-Myosin Light Chain Kinase Complex: Implications of Calmodulin Function Authors: Persechini, A. / Kretsinger, R.H. | ||||||
History |
| ||||||
Remark 650 | HELIX THERE IS A BEND OF 40 DEGREES BETWEEN THE F2 HELIX RESIDUES 66 - 76, AND THE LINKER 77 - 83. ...HELIX THERE IS A BEND OF 40 DEGREES BETWEEN THE F2 HELIX RESIDUES 66 - 76, AND THE LINKER 77 - 83. THE ANGLE BETWEEN THE LINKER AND THE E3 HELIX, 85 - 92, IS 85 DEGREES. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 16.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 7.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 287.3 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 287.3 KB | Display | |
Data in XML | ![]() | 857 B | Display | |
Data in CIF | ![]() | 2.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.990874, 0.076905, 0.110695), Vector: Details | THERE IS AN APPROXIMATE NON-CRYSTALLOGRAPHIC TWO-FOLD AXIS ROUGHLY PARALLEL TO B, RELATING DOMAIN I, (RESIDUES 12 - 74) AND DOMAIN II (RESIDUES 85 - 147). THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR DOMAIN I WHEN APPLIED TO DOMAIN II. | |
-
Components
#1: Protein | Mass: 16034.614 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() | ||
---|---|---|---|
#2: Chemical | ChemComp-CA / Sequence details | SEQUENCE ADVISORY NOTICE DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. SWISS-PROT ENTRY NAME: ...SEQUENCE ADVISORY NOTICE DIFFERENCE | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 44.06 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6.1 / Method: vapor diffusion | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.9 Å / Num. all: 3483 / Num. obs: 3396 / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rmerge(I) obs: 0.09 |
Reflection shell | *PLUS Highest resolution: 2.9 Å / Lowest resolution: 3.1 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.115 / Mean I/σ(I) obs: 5.3 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor Rwork: 0.23 / Rfactor obs: 0.23 / Highest resolution: 2.9 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.9 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|