5D0I: RING finger protein 165

Structure of RING finger protein 165. Determined by X-ray diffraction at 1.9 Å resolution. Released 9 Dec 2015.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
2
Atoms
963
Mol. weight
22.39 kDa
Ligands
ZN
Released
9 Dec 2015

Explore 5D0I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5D0I contains 7 α-helices and 13 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: 4 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix261-2644
β-strand266-26941
β-strand29312
α-helix2991
β-strand30012
α-helix3011
β-strand306-30941
β-strand315-31731
α-helix318-32811
β-strand33013
β-strand33713
Chain B: 3 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand29314
β-strand30014
β-strand307-30935
β-strand315-31735
α-helix318-32710
β-strand33016
α-helix3361
β-strand33716
α-helix338-3392

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RING finger protein 165A, Bprotein97Homo sapiensQ6ZSG1 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5D0I_1 RING finger protein 165 (chains A, B)
GPLGSGAVQNTIERFTFPHKYKKRRPQDGKGKKDEGEESDTDEKCTICLSMLEDGEDVRR
LPCMHLFHQLCVDQWLAMSKKCPICRVDIETQLGADS

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

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

Primary citation

Secondary ubiquitin-RING docking enhances Arkadia and Ark2C E3 ligase activity. Wright, J.D., Mace, P.D., Day, C.L. Nat Struct Mol Biol (2016) 23:45-52. DOI 10.1038/nsmb.3142 · PubMed

Other PDB entries of the same protein (UniProt Q6ZSG1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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