1YVN: Protein

The yeast actin val 159 asn mutant complex with human gelsolin segment 1. Determined by X-ray diffraction at 2.1 Å resolution. Released 23 Mar 2000.

Method
X-ray diffraction
Resolution
2.1 Å
Organisms
Saccharomyces cerevisiae, Homo sapiens
Chains
2
Atoms
4,190
Mol. weight
56.49 kDa
Ligands
CA, ATP, MG
Released
23 Mar 2000

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

Secondary structure: helices and β-sheets

1YVN contains 30 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: 24 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
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-helix182-19514
α-helix203-21614
α-helix223-2319
β-strand238-24146
β-strand247-25046
α-helix253-2564
α-helix258-2614
α-helix264-2674
α-helix274-28310
α-helix287-2959
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
>1YVN_1 PROTEIN (ACTIN) (chains A)
MDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQS
KRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMT
QIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGNTHVVPIYAGFSLPHAILRIDL
AGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSY
ELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMS
GGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQ
EYDESGPSIVHHKCF
Sequence of entity 2 (G), FASTA
>1YVN_2 PROTEIN (GELSOLIN) (chains G)
MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYD
LHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGG
VASGF

Ligands and cofactors

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

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

Primary citation

Crystal structure of yeast actin V159N mutant. Vorobiev, S.M., Belmont, L.D., Drubin, D.D. et al. To be published.

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

Browse structure collections

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