1B9A
PARVALBUMIN (MUTATION;D51A, F102W)
Summary for 1B9A
Entry DOI | 10.2210/pdb1b9a/pdb |
Descriptor | PROTEIN (PARVALBUMIN), CALCIUM ION (3 entities in total) |
Functional Keywords | calcium binding protein, ef-hand proteins, parvalbumin, calcium-binding |
Biological source | Cyprinus carpio (common carp) |
Total number of polymer chains | 1 |
Total formula weight | 11525.97 |
Authors | Cates, M.S.,Berry, M.B.,Ho, E.L.,Li, Q.,Potter, J.D.,Phillips Jr., G.N. (deposition date: 1999-02-10, release date: 1999-02-15, Last modification date: 2023-08-09) |
Primary citation | Cates, M.S.,Berry, M.B.,Ho, E.L.,Li, Q.,Potter, J.D.,Phillips Jr., G.N. Metal-ion affinity and specificity in EF-hand proteins: coordination geometry and domain plasticity in parvalbumin. Structure Fold.Des., 7:1269-1278, 1999 Cited by PubMed Abstract: The EF-hand family is a large set of Ca(2+)-binding proteins that contain characteristic helix-loop-helix binding motifs that are highly conserved in sequence. Members of this family include parvalbumin and many prominent regulatory proteins such as calmodulin and troponin C. EF-hand proteins are involved in a variety of physiological processes including cell-cycle regulation, second messenger production, muscle contraction, microtubule organization and vision. PubMed: 10545326DOI: 10.1016/S0969-2126(00)80060-X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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