4KSJ: OTU domain of Gumby/Fam105B

Crystal structure of the OTU domain of Gumby/Fam105B at 1.6 angstrom. Determined by X-ray diffraction at 1.6 Å resolution. Released 5 Jun 2013.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Homo sapiens
Chains
1
Atoms
2,326
Mol. weight
32.76 kDa
Released
5 Jun 2013

Explore 4KSJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4KSJ contains 19 α-helices and 11 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: 19 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand8211
α-helix83-853
β-strand86-8722
α-helix88-958
α-helix101-11414
β-strand119-12132
α-helix1221
β-strand12311
α-helix1241
α-helix129-14012
α-helix147-1504
α-helix153-16412
α-helix166-1705
α-helix184-20320
α-helix208-21811
α-helix223-24826
α-helix255-2628
α-helix269-2757
α-helix277-2793
β-strand28013
β-strand28413
α-helix288-29811
β-strand301-30664
α-helix307-3093
α-helix313-3153
β-strand316-31944
α-helix3281
β-strand329-33464
β-strand340-34124
β-strand342-34432

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein FAM105BAprotein276Homo sapiensQ96BN8 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4KSJ_1 Protein FAM105B (chains A)
GSRLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFTSIRRVRGDNYCALRATLF
QAMSQAVGLPPWLQDPELMLLPEKLISKYNWIKQWKLGLKFDGKNEDLVDKIKESLTLLR
KKWAGLAEMRTAEARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYNDKEKGKEVPFF
SVLLFARDTSNDPGQLLRNHLNQVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFI
TVYPTDPPKDWPVVTLIAEDDRHYNIPVRVCEETSL

Primary citation

The linear ubiquitin-specific deubiquitinase gumby regulates angiogenesis. Rivkin, E., Almeida, S.M., Ceccarelli, D.F. et al. Nature (2013) 498:318-324. DOI 10.1038/nature12296 · PubMed

Other PDB entries of the same protein (UniProt Q96BN8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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