1HVG

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

Summary for 1HVG

DescriptorANNEXIN V (1 entity in total)
Functional Keywordscalcium/phospholipid binding, calcium-phospholipid binding complex
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total molecular weight35848.53
Authors
Burger, A.,Huber, R. (deposition date: 1994-06-29, release date: 1995-03-31, Last modification date: 2011-07-13)
Primary citation
Burger, A.,Voges, D.,Demange, P.,Perez, C.R.,Huber, R.,Berendes, R.
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
J.Mol.Biol., 237:479-499, 1994
PubMed: 8151707 (PDB entries with the same primary citation)
DOI: 10.1006/jmbi.1994.1249
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (3 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers91.0%10.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report