3LMN: Ubiquitin carboxyl-terminal hydrolase 15

Name: PDB 3LMN: Oligomeric structure of the DUSP domain of human USP15
Published: 2010-03-23
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: hydrolase

Oligomeric structure of the DUSP domain of human USP15. Determined by X-ray diffraction at 2.15 Å resolution. Released 23 Mar 2010.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,373
Mol. weight: 31.16 kDa
Released: 23 Mar 2010

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

Secondary structure: helices and β-sheets

3LMN contains 19 α-helices and 16 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: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	7-8	2
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
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
α-helix	107	1
β-strand	114-116	3	1

Chain B: 10 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
α-helix	9-19	11
α-helix	22-24	3
β-strand	29-34	6	4
α-helix	35-45	11
α-helix	49-51	3
α-helix	58-60	3
β-strand	65	1	5
α-helix	68-70	3
β-strand	71-72	2	6
β-strand	78-79	2	6
α-helix	80	1
β-strand	85	1	4
β-strand	89-93	5	4
α-helix	94-104	11
β-strand	106	1	5
α-helix	107	1
β-strand	114-116	3	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin carboxyl-terminal hydrolase 15	A, B	protein	135	Homo sapiens	Q9Y4E8 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3LMN_1 Ubiquitin carboxyl-terminal hydrolase 15 (chains A, B)
GSMAEGGAADLDTQRSDIATLLKTSLRKGDTWYLVDSRWFKQWKKYVGFDSWDKYQMGDQ
NVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYTLMEGQEPIARKVV
EQGMFVKHCKVEVYL

Primary citation

Crystal Structure of the Human Ubiquitin-Specific Protease 15 DUSP Domain. Walker, J.R., Asinas, A., Avvakumov, G.V. 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
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

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