5W0G: U2AF65 (U2AF2) RRM1 at 1.07 resolution

Structure of U2AF65 (U2AF2) RRM1 at 1.07 resolution. Determined by X-ray diffraction at 1.07 Å resolution. Released 11 Apr 2018.

Method
X-ray diffraction
Resolution
1.07 Å
Organism
Homo sapiens
Chains
1
Atoms
859
Mol. weight
10.07 kDa
Ligands
1PG, ZN
Released
11 Apr 2018

Explore 5W0G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5W0G contains 5 α-helices and 6 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: 5 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix147-1493
β-strand150-15451
α-helix156-1572
α-helix162-17514
β-strand186-19161
β-strand197-20261
α-helix205-2117
α-helix212-2143
β-strand218-21922
β-strand222-22322
β-strand225-22731

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Splicing factor U2AF 65 kDa subunitAprotein87Homo sapiensP26368 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5W0G_1 Splicing factor U2AF 65 kDa subunit (chains A)
GPLGSARRLYVGNIPFGITEEAMMDFFNAQMRLGGLTQAPGNPVLAVQINQDKNFAFLEF
RSVDETTQAMAFDGIIFQGQSLKIRRP

Ligands and cofactors

IDNameFormulaCopies
1PG2-(2-{2-[2-(2-methoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethanolC11 H24 O61
ZNZinc ionZn2

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

Primary citation

Cancer-Associated Mutations Mapped on High-Resolution Structures of the U2AF2 RNA Recognition Motifs. Glasser, E., Agrawal, A.A., Jenkins, J.L. et al. Biochemistry (2017) 56:4757-4761. DOI 10.1021/acs.biochem.7b00551 · PubMed

Other PDB entries of the same protein (UniProt P26368 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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