6GHA: USP15 catalytic domain structure

USP15 catalytic domain structure. Determined by X-ray diffraction at 1.98 Å resolution. Released 26 Sept 2018.

Method: X-ray diffraction
Resolution: 1.98 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,734
Mol. weight: 41.81 kDa
Ligands: ZN
Released: 26 Sept 2018

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

Secondary structure: helices and β-sheets

6GHA contains 14 α-helices and 19 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: 14 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	261-262	2	1
α-helix	271-279	9
α-helix	282-289	8
α-helix	294-296	3
α-helix	308-320	13
β-strand	327-328	2	1
α-helix	331-340	10
α-helix	355-366	12
α-helix	373-375	3
α-helix	386-400	15
α-helix	404-409	6
β-strand	411-418	8	2
β-strand	425-432	8	2
β-strand	435-437	3	3
β-strand	756-758	3	4
α-helix	759-766	8
β-strand	770-771	2	2
α-helix	772-773	2
β-strand	778-780	3	5
β-strand	785-787	3	5
β-strand	790-797	8	2
β-strand	801-806	6	3
β-strand	822-824	3	4
β-strand	830-831	2	3
α-helix	833-835	3
β-strand	836	1	2
β-strand	845-855	11	3
β-strand	862-868	7	3
β-strand	875-879	5	3
β-strand	882-885	4	3
α-helix	888-890	3
β-strand	896-903	8	3
α-helix	904-906	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin carboxyl-terminal hydrolase 15,Ubiquitin carboxyl-terminal hydrolase 15	A	protein	365	Homo sapiens	Q9Y4E8 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6GHA_1 Ubiquitin carboxyl-terminal hydrolase 15,Ubiquitin carboxyl-terminal hydrolase 15 (chains A)
MEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRGEIAKSY
AELIKQMWSGKFSYVTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKK
PYIQLKDADGRPDKVVAEEAWENHLKRNDSIIVDIFHGLFKSTLVCPECAKISVTFDPFC
YLTLPLASTSKVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVH
LKRFSYSRYMRDKLDTLVDFPINDLDMSEFLINPNAGPCRYNLIAVSNHYGGMGGGHYTA
FAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQRQDTFSGTGFFPLDRETAAALEH
HHHHH

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

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:

4A3P 1.4 Å, Structure of USP15 DUSP-UBL deletion mutant
3T9L 1.5 Å, Structure of N-terminal DUSP-UBL domains of human USP15
6ML1 1.9 Å, Structure of the USP15 deubiquitinase domain in complex with an affinity-matured…
7R2G 1.98 Å, USP15 D1D2 in catalytically-competent state bound to mitoxantrone stack (isoform 2)
6CPM 2.01 Å, Structure of the USP15 deubiquitinase domain in complex with a third-generation…
6GH9 2.09 Å, USP15 catalytic domain in complex with small molecule
3LMN 2.15 Å, Oligomeric structure of the DUSP domain of human USP15
4A3O 2.2 Å, Crystal structure of the USP15 DUSP-UBL monomer
9VVV 2.3 Å, Crystal structure of USP15 catalytic domain in complex with Ub-PA
3PPA 2.35 Å, Structure of the Dusp-Ubl domains of Usp15
6CRN 2.5 Å, Structure of the USP15 deubiquitinase domain in complex with a high-affinity…
3PV1 2.6 Å, Crystal structure of the USP15 DUSP-UBL domains

Browse structure collections

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