7F0N: Deamidated Ubiquitin

Structure of deamidated Ubiquitin. Determined by X-ray diffraction at 1.6 Å resolution. Released 8 Jun 2022.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Homo sapiens
Chains
1
Atoms
792
Mol. weight
8.87 kDa
Ligands
MG
Released
8 Jun 2022

Explore 7F0N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7F0N contains 5 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: 5 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand2-651
β-strand12-1651
β-strand2212
α-helix23-3412
α-helix38-403
β-strand41-4551
β-strand48-4921
α-helix50-512
β-strand5512
α-helix57-593
β-strand66-7161
α-helix73-753

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-40S ribosomal protein S27aAprotein76Homo sapiensP62979 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>7F0N_1 Ubiquitin-40S ribosomal protein S27a (chains A)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDEQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

Water and common crystallization additives (K, NA) are not listed.

Primary citation

Structure of deamidated Ubiquitin. Rashmi, R., Mohanty, P., Aravind, R. et al. To be published.

Other PDB entries of the same protein (UniProt P62979 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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