1OGW: Synthetic Ubiquitin with fluoro-Leu at 50 and 67

Synthetic Ubiquitin with fluoro-Leu at 50 and 67. Determined by X-ray diffraction at 1.32 Å resolution. Released 30 May 2003.

Method
X-ray diffraction
Resolution
1.32 Å
Organism
HOMO SAPIENS
Chains
1
Atoms
733
Mol. weight
8.61 kDa
Released
30 May 2003

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

Secondary structure: helices and β-sheets

1OGW contains 4 α-helices and 7 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: 4 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand2-761
β-strand12-1651
β-strand2212
α-helix23-3412
α-helix38-403
β-strand41-4551
β-strand48-4921
α-helix50-512
β-strand5512
α-helix56-594
β-strand66-7161

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
UbiquitinAprotein76HOMO SAPIENSP0CG48 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1OGW_1 UBIQUITIN (chains A)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Primary citation

Synthesis, Structural and Biological Studies of Ubiquitin Mutants Containing (2S, 4S)-5-Fluoroleucine Residues Strategically Placed in the Hydrophobic Core. Alexeev, D., Barlow, P.N., Bury, S.M. et al. Chembiochem (2003) 4:894. DOI 10.1002/CBIC.200300699 · PubMed

Other PDB entries of the same protein (UniProt P0CG48 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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