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
The structure was published by Burger, A., Voges, D., Demange, P., Perez, C.R., Huber, R., and Berendes, R., in 1994 in a paper entitled "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" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 1994.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of ANNEXIN V. This molecule has the UniProt identifier P08758 (ANXA5_HUMAN). The sample contained 319 residues which is 100% of the natural sequence. Out of 319 residues 313 were observed and are deposited in the PDB.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: