2EC4: UAS domain from human FAS-associated factor 1

Solution structure of the UAS domain from human FAS-associated factor 1. Determined by solution NMR. Released 4 Mar 2008.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,374
Mol. weight
20.13 kDa
Released
4 Mar 2008

Explore 2EC4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2EC4 contains 7 α-helices and 4 β-strands across 1 chain. 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: 7 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix13-2816
α-helix40-456
β-strand57-6371
α-helix69-768
α-helix81-899
β-strand91-9771
α-helix101-11414
α-helix117-1259
β-strand133-13751
β-strand146-15051
α-helix156-17318

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
FAS-associated factor 1Aprotein178Homo sapiensQ9UNN5 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2EC4_1 FAS-associated factor 1 (chains A)
GSSGSSGENAENEGDALLQFTAEFSSRYGDCHPVFFIGSLEAAFQEAFYVKARDRKLLAI
YLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKDSNRARFLTMCNRHFGSVVA
QTIRTQKTDQFPLFLIIMGKRSSNEVLNVIQGNTTVDELMMRLMAAMEIFTAQQQEDI

Primary citation

Solution structure of the UAS domain from human FAS-associated factor 1. Zhang, H.P., Hayashi, F., Yokoyama, S. To be published.

Other PDB entries of the same protein (UniProt Q9UNN5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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