3PPA: Dusp-Ubl domains of Usp15

Structure of the Dusp-Ubl domains of Usp15. Determined by X-ray diffraction at 2.35 Å resolution. Released 19 Jan 2011.

Method: X-ray diffraction
Resolution: 2.35 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,668
Mol. weight: 27.9 kDa
Ligands: CIT
Released: 19 Jan 2011

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

Secondary structure: helices and β-sheets

3PPA contains 9 α-helices and 17 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, 17 β-strands

Element	Residues	Length	Sheet
α-helix	10-19	10
α-helix	22-24	3
β-strand	29-34	6	1
α-helix	35-45	11
β-strand	48	1	2
β-strand	51	1	2
β-strand	65	1	3
β-strand	71	1	4
α-helix	78	1
β-strand	79	1	4
α-helix	80	1
β-strand	85	1	1
β-strand	89-93	5	1
α-helix	94-104	11
β-strand	106	1	3
β-strand	114-116	3	1
α-helix	133	1
β-strand	134-140	7	5
β-strand	148-152	5	5
β-strand	157	1	6
α-helix	158-168	11
β-strand	177-182	6	5
β-strand	188-190	3	5
β-strand	197	1	6
β-strand	208-213	6	5
α-helix	214-215	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin carboxyl-terminal hydrolase 15	A	protein	237	Homo sapiens	Q9Y4E8 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3PPA_1 Ubiquitin carboxyl-terminal hydrolase 15 (chains A)
MGSSHHHHHHSSGLVPRGSAADLDTQRSDIATLLKTSLRKGDTWYLVDSRWFKQWKKYVG
FDSWDKYQMGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYTL
MEGQEPIARKVVEQGMFVKHCKVEVYLTELKLCENGNMNNVVTRRFSKADTIDTIEKEIR
KIFSIPDEKETRLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQKNEDGTWPRG

Ligands and cofactors

ID	Name	Formula	Copies
CIT	Citric acid	C6 H8 O7	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structure of the Dusp-Ubl Domains of the Ubiquitin-Specific Protease 15. Walker, J.R., Asinas, A.E., Dong, A. et al. To be published.

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
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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