3PV1: USP15 DUSP-UBL domains

Crystal structure of the USP15 DUSP-UBL domains. Determined by X-ray diffraction at 2.6 Å resolution. Released 16 Nov 2011.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,625
Mol. weight: 51.97 kDa
Released: 16 Nov 2011

Explore 3PV1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3PV1 contains 18 α-helices and 30 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: 11 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	9-19	11
α-helix	22-24	3
β-strand	29-34	6	1
α-helix	35-45	11
α-helix	58-60	3
β-strand	65	1	2
α-helix	68-70	3
β-strand	71	1	3
β-strand	79	1	3
α-helix	80	1
β-strand	85	1	1
β-strand	89-93	5	1
α-helix	94-104	11
β-strand	106	1	2
β-strand	114-130	17	1
α-helix	133	1
β-strand	134-140	7	4
β-strand	148-152	5	4
β-strand	157	1	5
α-helix	158-168	11
β-strand	177-184	8	4
β-strand	187-190	4	4
β-strand	197	1	5
α-helix	198-201	4
β-strand	208-213	6	4
α-helix	214-215	2

Chain B: 7 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	9-19	11
β-strand	29-34	6	1
α-helix	35-45	11
β-strand	65	1	6
α-helix	68-70	3
β-strand	71	1	7
β-strand	79	1	7
β-strand	85	1	1
β-strand	89-93	5	1
α-helix	94-104	11
β-strand	106	1	6
β-strand	114-130	17	1
α-helix	133	1
β-strand	134-140	7	8
β-strand	143-152	10	8
β-strand	157	1	9
α-helix	158-168	11
β-strand	177-182	6	8
β-strand	188-190	3	8
β-strand	197	1	9
β-strand	208-213	6	8
α-helix	214-215	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin carboxyl-terminal hydrolase 15	A, B	protein	225	Homo sapiens	Q9Y4E8 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3PV1_1 Ubiquitin carboxyl-terminal hydrolase 15 (chains A, B)
GAMAEGGAADLDTQRSDIATLLKTSLRKGDTWYLVDSRWFKQWKKYVGFDSWDKYQMGDQ
NVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYTLMEGQEPIARKVV
EQGMFVKHCKVEVYLTELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFSIPDEKETR
LWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQKNEDGTWPRG

Primary citation

Structural variability of the ubiquitin specific protease DUSP-UBL double domains. Elliott, P.R., Liu, H., Pastok, M.W. et al. FEBS Lett (2011) 585:3385-3390. DOI 10.1016/j.febslet.2011.09.040 · 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…
6GHA 1.98 Å, USP15 catalytic domain structure
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…

Browse structure collections

About this viewer

MolViewer shows 3PV1 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.