4UEM: UCH-L5

UCH-L5 in complex with the RPN13 DEUBAD domain. Determined by X-ray diffraction at 2.82 Å resolution. Released 4 Mar 2015.

Method: X-ray diffraction
Resolution: 2.82 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 2,989
Mol. weight: 50.8 kDa
Released: 4 Mar 2015

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

Secondary structure: helices and β-sheets

4UEM contains 25 α-helices and 13 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: 16 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3
α-helix	15-24	10
β-strand	28	1	1
β-strand	30-35	6	2
α-helix	40-43	4
β-strand	49-56	8	2
α-helix	62-64	3
β-strand	68	1	2
α-helix	73-76	4
α-helix	85-87	3
α-helix	88-97	10
β-strand	106	1	1
α-helix	108-118	11
α-helix	123-131	9
α-helix	134-142	9
α-helix	144-146	3
β-strand	165-171	7	2
β-strand	174-179	6	2
β-strand	186-190	5	2
β-strand	192	1	3
β-strand	195	1	3
α-helix	197-209	13
β-strand	218-225	8	2
α-helix	227-243	17
α-helix	255-288	34
α-helix	292-304	13
α-helix	308-314	7

Chain B: 9 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	288-291	4
α-helix	298-301	4
α-helix	304-310	7
α-helix	311-313	3
β-strand	317	1	4
β-strand	320	1	4
α-helix	325-331	7
α-helix	334-348	15
α-helix	353-358	6
α-helix	363-371	9
α-helix	374-383	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin carboxyl-terminal hydrolase isozyme L5	A	protein	331	HOMO SAPIENS	Q9Y5K5 (AlphaFold model)
Proteasomal ubiquitin receptor ADRM1	B	protein	127	HOMO SAPIENS	Q16186 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4UEM_1 UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5 (chains A)
GPGMTGNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFK
WQPGEEPAGSVVQDSRLDTIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEF
SQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYE
LDGLREGPIDLGACNQDDWISAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAE
LQRQLAEEPMDTDQGNSMLSAIQSEVAKNQMLIEEEVQKLKRYKIENIRRKHNYLPFIME
LLKTLAEHQQLIPLVEKAKEKQNAKKAQETK

Sequence of entity 2 (B), FASTA

>4UEM_2 PROTEASOMAL UBIQUITIN RECEPTOR ADRM1 (chains B)
GPGSDLQSILATMNVPAGPAGGQQVDLASVLTPEIMAPILANADVQERLLPYLPSGESLP
QTADEIQNTLTSPQFQQALGMFSAALASGQLGPLMCQFGLPAEAVEAANKGDVEAFAKAM
QNNAKPE

Primary citation

Mechanism of Uch-L5 Activation and Inhibition by Deubad Domains in Rpn13 and Ino80G. Sahtoe, D.D., Van Dijk, W.J., El Oualid, F. et al. Mol Cell (2015) 57:887. DOI 10.1016/J.MOLCEL.2014.12.039 · PubMed

Other PDB entries of the same protein (UniProt Q9Y5K5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3RII 2.0 Å, Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human…
3A7S 2.2 Å, Catalytic domain of UCH37
3TB3 2.3 Å, Crystal structure of the UCH domain of UCH-L5 with 6 residues deleted
4UEL 2.3 Å, UCH-L5 in complex with ubiquitin-propargyl bound to the RPN13 DEUBAD domain
3RIS 2.4 Å, Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human…
9E7K 2.41 Å, Crystal structure of the UCH37 RPN13 DEUBAD complex bound to an inhibitory nanobody in…
3IHR 2.95 Å, Crystal Structure of Uch37
4WLP 3.1 Å, Crystal structure of UCH37-NFRKB Inhibited Deubiquitylating Complex
4UF6 3.69 Å, UCH-L5 in complex with ubiquitin-propargyl bound to an activating fragment of INO80G
4UF5 3.7 Å, Crystal structure of UCH-L5 in complex with inhibitory fragment of INO80G

Browse structure collections

About this viewer

MolViewer shows 4UEM 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.