5MN9: MINDY-1 tMIU

Crystal structure of MINDY-1 tMIU in complex with K48-diUb. Determined by X-ray diffraction at 2.05 Å resolution. Released 25 Jan 2017.

Method
X-ray diffraction
Resolution
2.05 Å
Organisms
Bos taurus, Homo sapiens
Chains
3
Atoms
1,335
Mol. weight
22.09 kDa
Released
25 Jan 2017

Explore 5MN9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5MN9 contains 9 α-helices and 14 β-strands across 3 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.

Chains A and B: 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-helix57-593
β-strand66-7161
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix411-42515

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-40S ribosomal protein S27aA, Bprotein76Bos taurusP62992 (AlphaFold model)
Ubiquitin carboxyl-terminal hydrolase MINDY-1Cprotein44Homo sapiensQ8N5J2 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5MN9_1 Ubiquitin-40S ribosomal protein S27a (chains A, B)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG
Sequence of entity 2 (C), FASTA
>5MN9_2 Ubiquitin carboxyl-terminal hydrolase MINDY-1 (chains C)
GPLGSQVDQDYLIALSLQQQQPRGPLGLTDLELAQQLQQEEYQQ

Primary citation

A single MIU motif of MINDY-1 recognizes K48-linked polyubiquitin chains. Kristariyanto, Y.A., Abdul Rehman, S.A., Weidlich, S. et al. EMBO Rep (2017) 18:392-402. DOI 10.15252/embr.201643205 · PubMed

Other PDB entries of the same protein (UniProt P62992 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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