4A3O: USP15 DUSP-UBL monomer

Crystal structure of the USP15 DUSP-UBL monomer. Determined by X-ray diffraction at 2.2 Å resolution. Released 16 Nov 2011.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 3,719
Mol. weight: 51.21 kDa
Released: 16 Nov 2011

Explore 4A3O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4A3O contains 20 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: 10 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	9-20	12
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
α-helix	79-80	2
β-strand	85	1	1
β-strand	89-93	5	1
α-helix	94-104	11
β-strand	106	1	2
α-helix	107	1
β-strand	114-116	3	1
β-strand	117-120	4	3
β-strand	126-129	4	3
α-helix	133	1
β-strand	134-140	7	4
β-strand	143-152	10	4
β-strand	157	1	5
α-helix	158-168	11
β-strand	177-183	7	4
β-strand	187-190	4	4
β-strand	197	1	5
β-strand	208-213	6	4

Chain B: 10 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	9-19	11
α-helix	22-24	3
β-strand	29-34	6	6
α-helix	35-45	11
α-helix	58-60	3
β-strand	65	1	7
α-helix	68-70	3
α-helix	79-80	2
β-strand	85	1	6
β-strand	89-93	5	6
α-helix	94-104	11
β-strand	106	1	7
α-helix	107	1
β-strand	114-116	3	6
β-strand	117-120	4	8
β-strand	126-129	4	8
α-helix	133	1
β-strand	134-140	7	9
β-strand	148-152	5	9
β-strand	157	1	10
α-helix	158-168	11
β-strand	177-183	7	9
β-strand	187-190	4	9
β-strand	197	1	10
β-strand	208-213	6	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin carboxyl-terminal hydrolase 15	A, B	protein	220	HOMO SAPIENS	Q9Y4E8 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4A3O_1 UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15 (chains A, B)
GAAADLDTQRSDIATLLKTSLRKGDTWYLVDSRWFKQWKKYVGFDSWDKYQMGDQNVYPG
PIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYTLMEGQEPIARKVVEQGMF
VKHCKVEVYLTELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFSIPDEKETRLWNKY
MSNTFEPLNKPDSTIQDAGLYQGQVLVIEQKNEDGTWPRG

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. 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
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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