3N3K: The catalytic domain of USP8

The catalytic domain of USP8 in complex with a USP8 specific inhibitor. Determined by X-ray diffraction at 2.6 Å resolution. Released 23 Jun 2010.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Homo sapiens
Chains
2
Atoms
3,601
Mol. weight
54.75 kDa
Ligands
ZN
Released
23 Jun 2010

Explore 3N3K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3N3K contains 21 α-helices and 35 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: 17 helices, 25 β-strands

ElementResiduesLengthSheet
α-helix759-7657
α-helix7671
β-strand768-76921
β-strand778-77921
α-helix786-79611
α-helix801-8066
α-helix809-8124
α-helix825-83915
β-strand842-84541
α-helix848-85710
β-strand85812
α-helix859-8613
α-helix869-88315
α-helix903-91715
α-helix921-9266
β-strand928-93693
β-strand942-94543
β-strand948-94923
β-strand952-95434
α-helix955-9562
β-strand961-96335
α-helix964-9718
β-strand975-97733
α-helix979-9813
α-helix9821
β-strand983-98536
β-strand990-99236
β-strand994-100293
β-strand1006-101164
β-strand1014-101637
β-strand1021-102337
β-strand1027-102935
β-strand103518
α-helix1038-10403
β-strand104113
β-strand105118
β-strand1052-106094
β-strand1067-107484
β-strand1079-108464
β-strand1087-109044
α-helix1093-10953
β-strand1101-110774
Chain B: 4 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand2-769
α-helix8-103
β-strand11-1669
β-strand22110
α-helix23-3412
α-helix38-403
β-strand41-4559
β-strand4712
β-strand48-4929
α-helix50-512
β-strand52111
β-strand54111
β-strand55110
β-strand66-7169

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin carboxyl-terminal hydrolase 8Aprotein396Homo sapiensP40818 (AlphaFold model)
UbiquitinBprotein85Homo sapiensP0CG48 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3N3K_1 Ubiquitin carboxyl-terminal hydrolase 8 (chains A)
MGSSHHHHHHSSGLVPRGSPTVTPTVNRENKPTCYPKAEISRLSASQIRNLNPVFGGSGP
ALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIM
KALWTGQYRYISPKDFKITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKADNRKRYK
EENNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMYLSL
PLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRF
SYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKN
AARQRWFKFDDHEVSDISVSSVKSSAAYILFYTSLG
Sequence of entity 2 (B), FASTA
>3N3K_2 Ubiquitin (chains B)
GSHMRIVVKTLMGRTIILEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLS
DYNIHNHSALYLLLKLRGGGGGGSG

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

Primary citation

A strategy for modulation of enzymes in the ubiquitin system. Ernst, A., Avvakumov, G., Tong, J. et al. Science (2013) 339:590-595. DOI 10.1126/science.1230161 · PubMed

Other PDB entries of the same protein (UniProt P40818 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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