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From Proteopedia

1esv, resolution 2.00Å ()
Sites:	, , , and
Ligands:	, ,
Non-Standard Residues:
Related:	1eqy
Structural annotation: Resources: CATH : 1Esva04, 1Esva01, 1Esva02, 1Esva03, 1Esvs00 InterPro : Ipr004000, Ipr004001, Ipr007122, Ipr007123 Pfam : PF00022, PF00626 SCOP : d1esva2, d1esva1, d1esvs_ UniProt : P68135, P06396
Functional annotation: Cellular component: cytoplasm stress fiber cytoskeleton actin filament striated muscle thin filament extracellular region cytosol actin cytoskeleton Biological process: muscle thin filament assembly skeletal muscle fiber development actin filament severing barbed-end actin filament capping actin filament polymerization Molecular function: structural molecule activity protein binding nucleotide binding ATP binding calcium ion binding actin binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

COMPLEX BETWEEN LATRUNCULIN A:RABBIT MUSCLE ALPHA ACTIN:HUMAN GELSOLIN DOMAIN 1

About this Structure

1esv is a 2 chain structure of Actin and Gelsolin with sequence from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA.

See Also

• Actin
• Gelsolin

Reference

• Morton WM, Ayscough KR, McLaughlin PJ. Latrunculin alters the actin-monomer subunit interface to prevent polymerization. Nat Cell Biol. 2000 Jun;2(6):376-8. PMID:10854330 doi:10.1038/35014075