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Yorodumi- PDB-1hvg: STRUCTURAL AND ELECTROPHYSIOLOGICAL ANALYSIS OF ANNEXIN V MUTANTS... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hvg | ||||||
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Title | STRUCTURAL AND ELECTROPHYSIOLOGICAL ANALYSIS OF ANNEXIN V MUTANTS. MUTAGENESIS OF HUMAN ANNEXIN V, AN IN VITRO VOLTAGE-GATED CALCIUM CHANNEL, PROVIDES INFORMATION ABOUT THE STRUCTURAL FEATURES OF THE ION PATHWAY, THE VOLTAGE SENSOR AND THE ION SELECTIVITY FILTER | ||||||
Components | ANNEXIN VAnnexin A5 | ||||||
Keywords | CALCIUM/PHOSPHOLIPID BINDING / CALCIUM-PHOSPHOLIPID BINDING complex | ||||||
Function / homology | Function and homology information phospholipase inhibitor activity / endothelial microparticle / negative regulation of coagulation / calcium-dependent phospholipid binding / phosphatidylserine binding / : / phospholipid binding / sarcolemma / blood coagulation / Platelet degranulation ...phospholipase inhibitor activity / endothelial microparticle / negative regulation of coagulation / calcium-dependent phospholipid binding / phosphatidylserine binding / : / phospholipid binding / sarcolemma / blood coagulation / Platelet degranulation / collagen-containing extracellular matrix / external side of plasma membrane / focal adhesion / calcium ion binding / negative regulation of apoptotic process / signal transduction / extracellular exosome / extracellular region / membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 3 Å | ||||||
Authors | Burger, A. / Huber, R. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1994 Title: Structural and electrophysiological analysis of annexin V mutants. Mutagenesis of human annexin V, an in vitro voltage-gated calcium channel, provides information about the structural features ...Title: Structural and electrophysiological analysis of annexin V mutants. Mutagenesis of human annexin V, an in vitro voltage-gated calcium channel, provides information about the structural features of the ion pathway, the voltage sensor and the ion selectivity filter Authors: Burger, A. / Voges, D. / Demange, P. / Perez, C.R. / Huber, R. / Berendes, R. #1: Journal: J.Mol.Biol. / Year: 1992 Title: Crystal and Molecular Structure of Human Annexin V After Refinement Authors: Huber, R. / Berendes, R. / Burger, A. / Schneider, M. / Karshikov, A. / Luecke, H. / Romish, J. / Paques, E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hvg.cif.gz | 71.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hvg.ent.gz | 53.6 KB | Display | PDB format |
PDBx/mmJSON format | 1hvg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hv/1hvg ftp://data.pdbj.org/pub/pdb/validation_reports/hv/1hvg | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 35848.527 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line: 293 / Gene: CDNA / Organ: PLACENTA UNFUSED / Plasmid: PTRC 99A-PP4 GENE: CDNA / Production host: Escherichia coli (E. coli) / Strain (production host): 293 / References: UniProt: P08758 |
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Compound details | THE STRUCTURAL ANALYSIS SHOULD REVEAL WHETHER THE STRUCTURAL REARRANGEMENT IN DOMAIN III AS SEEN IN ...THE STRUCTURAL |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49.55 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 8.5 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Highest resolution: 3 Å / Num. obs: 5103 / % possible obs: 75 % / Observed criterion σ(I): 0 |
Reflection | *PLUS Lowest resolution: 9999 Å / Num. measured all: 17631 / Rmerge(I) obs: 0.073 |
Reflection shell | *PLUS Highest resolution: 3 Å / Lowest resolution: 3.11 Å / % possible obs: 44.1 % |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.199 / Rfactor obs: 0.199 / Highest resolution: 3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 3 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 8 Å / Num. reflection all: 4969 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |