6GH9: USP15 catalytic domain

USP15 catalytic domain in complex with small molecule. Determined by X-ray diffraction at 2.09 Å resolution. Released 26 Sept 2018.

Method
X-ray diffraction
Resolution
2.09 Å
Organism
Homo sapiens
Chains
2
Atoms
5,319
Mol. weight
84.08 kDa
Ligands
MIX, ZN
Released
26 Sept 2018

Explore 6GH9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6GH9 contains 25 α-helices and 36 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: 13 helices, 19 β-strands

ElementResiduesLengthSheet
β-strand261-26221
α-helix271-2799
α-helix282-2898
α-helix294-2963
α-helix308-32013
β-strand327-32821
α-helix331-34010
α-helix355-36612
α-helix373-3753
α-helix386-40015
α-helix404-4096
β-strand411-41992
β-strand424-43292
β-strand435-43733
β-strand757-75824
α-helix759-7668
β-strand770-77122
β-strand778-78035
β-strand785-78735
β-strand790-79782
β-strand801-80663
β-strand823-82424
β-strand830-83123
α-helix833-8353
β-strand83612
β-strand845-857133
β-strand860-86893
β-strand875-87953
β-strand882-88653
α-helix888-8914
β-strand896-90383
α-helix904-9063
Chain B: 12 helices, 17 β-strands
ElementResiduesLengthSheet
β-strand261-26226
α-helix271-2799
α-helix282-2898
α-helix294-2963
α-helix308-32013
β-strand327-32826
α-helix331-34010
α-helix355-36612
α-helix373-3753
α-helix386-40015
α-helix404-4096
β-strand411-41997
β-strand424-43297
β-strand435-43738
β-strand756-75839
α-helix759-7668
β-strand77017
β-strand790-79787
β-strand801-80668
β-strand822-82439
β-strand830-83128
β-strand83617
β-strand845-854108
β-strand863-86868
β-strand875-87958
β-strand882-88658
α-helix888-8903
β-strand896-90388
α-helix904-9063

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin carboxyl-terminal hydrolase 15A, Bprotein365Homo sapiensQ9Y4E8 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6GH9_1 Ubiquitin carboxyl-terminal hydrolase 15 (chains A, B)
MEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRGEIAKSY
AELIKQMWSGKFSYVTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKK
PYIQLKDADGRPDKVVAEEAWENHLKRNDSIIVDIFHGLFKSTLVCPECAKISVTFDPFC
YLTLPLASTSKVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVH
LKRFSYSRYMRDKLDTLVDFPINDLDMSEFLINPNAGPCRYNLIAVSNHYGGMGGGHYTA
FAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQRQDTFSGTGFFPLDRETAAALEH
HHHHH

Ligands and cofactors

IDNameFormulaCopies
MIX1,4-dihydroxy-5,8-BIS({2-[(2-hydroxyethyl)amino]ethyl}amino)-9,10-anthracenedio…C22 H28 N4 O61
ZNZinc ionZn1

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

Primary citation

The structure of the deubiquitinase USP15 reveals a misaligned catalytic triad and an open ubiquitin-binding channel. Ward, S.J., Gratton, H.E., Indrayudha, P. et al. J Biol Chem (2018) 293:17362-17374. DOI 10.1074/jbc.RA118.003857 · PubMed

Other PDB entries of the same protein (UniProt Q9Y4E8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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