1YAG: Yeast actin-human gelsolin segment 1 complex

Structure of the yeast actin-human gelsolin segment 1 complex. Determined by X-ray diffraction at 1.9 Å resolution. Released 9 Oct 1999.

Method
X-ray diffraction
Resolution
1.9 Å
Organisms
Saccharomyces cerevisiae, Homo sapiens
Chains
2
Atoms
4,348
Mol. weight
56.48 kDa
Ligands
MG, ATP, CA
Released
9 Oct 1999

Explore 1YAG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1YAG contains 31 α-helices and 28 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 25 helices, 21 β-strands

ElementResiduesLengthSheet
α-helix5-73
β-strand8-1251
β-strand16-2161
β-strand2212
β-strand2412
β-strand29-3241
β-strand35-3843
β-strand53-5423
α-helix56-605
α-helix62-643
β-strand65-6843
β-strand71-7224
β-strand75-7624
α-helix79-8810
α-helix89-946
α-helix98-1003
β-strand103-10751
α-helix113-1219
α-helix122-1265
β-strand131-13661
α-helix137-1448
β-strand150-15565
β-strand160-16675
β-strand169-17025
α-helix172-1743
β-strand176-17835
α-helix182-19413
α-helix203-21614
α-helix223-2286
β-strand238-24146
β-strand247-25046
α-helix253-2564
α-helix258-2614
α-helix264-2674
α-helix274-28310
α-helix287-2948
β-strand297-30045
α-helix302-3043
α-helix309-32012
β-strand329-33025
α-helix338-34811
α-helix350-3545
β-strand357-35821
α-helix359-3657
α-helix367-3693
α-helix370-3734
Chain G: 6 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix6-105
β-strand16-2387
β-strand26-2947
α-helix30-312
α-helix32-343
β-strand37-3938
β-strand43-5197
β-strand57-6597
α-helix71-8717
β-strand92-9877
α-helix104-1074
β-strand115-11738
α-helix122-1232

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein (ACTIN)Aprotein375Saccharomyces cerevisiaeP60010 (AlphaFold model)
Protein (gelsolin)Gprotein125Homo sapiensP06396 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1YAG_1 PROTEIN (ACTIN) (chains A)
MDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQS
KRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMT
QIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDL
AGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSY
ELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMS
GGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQ
EYDESGPSIVHHKCF
Sequence of entity 2 (G), FASTA
>1YAG_2 PROTEIN (GELSOLIN) (chains G)
MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYD
LHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGG
VASGF

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P31
CACalcium ionCa1

Water and common crystallization additives (SO4) are not listed.

Primary citation

The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism. Vorobiev, S., Strokopytov, B., Drubin, D.G. et al. Proc Natl Acad Sci U S A (2003) 100:5760-5765. DOI 10.1073/pnas.0832273100 · PubMed

Other PDB entries of the same protein (UniProt P60010 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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