6Z90: MINDY1 mutant-P138A

Crystal structure of MINDY1 mutant-P138A. Determined by X-ray diffraction at 3.59 Å resolution. Released 30 Jun 2021.

Method
X-ray diffraction
Resolution
3.59 Å
Organism
Homo sapiens
Chains
1
Atoms
1,946
Mol. weight
32.01 kDa
Released
30 Jun 2021

Explore 6Z90 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6Z90 contains 9 α-helices and 18 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: 9 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand113-12191
β-strand124-13071
β-strand13112
α-helix138-14811
β-strand160-16231
α-helix163-17412
α-helix189-20012
α-helix202-2054
β-strand21213
β-strand21314
β-strand22013
α-helix226-2327
β-strand236-23835
β-strand23916
α-helix247-2537
β-strand25714
α-helix260-2689
α-helix274-28815
β-strand29416
α-helix296-30510
β-strand312-31655
β-strand319-32575
β-strand330-33345
β-strand33612
β-strand347-34935
β-strand36015
β-strand36615

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin carboxyl-terminal hydrolase MINDY-1Aprotein289Homo sapiensQ8N5J2 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6Z90_1 Ubiquitin carboxyl-terminal hydrolase MINDY-1 (chains A)
GPLGSPEFPGRLEMEPDFYCVKWIPWKGEQTPIITQSTNGPCALLAIMNILFLQWKVKLP
PQKEVITSDELMAHLGNCLLSIKPQEKSEGLQLNFQQNVDDAMTVLPKLATGLDVNVRFT
GVSDFEYTPECSVFDLLGIPLYHGWLVDPQSPEAVRAVGKLSYNQLVERIITCKHSSDTN
LVTEGLIAEQFLETTAAQLTYHGLCELTAAAKEGELSVFFRNNHFSTMTKHKSHLYLLVT
DQGFLQEEQVVWESLHNVDGDSCFCDSDFHLSHSLGKGPGAEGGSGSPE

Primary citation

Mechanism of activation and regulation of deubiquitinase activity in MINDY1 and MINDY2. Abdul Rehman, S.A., Armstrong, L.A., Lange, S.M. et al. Mol Cell (2021) 81:4176-4190.e6. DOI 10.1016/j.molcel.2021.08.024 · PubMed

Other PDB entries of the same protein (UniProt Q8N5J2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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