4UEL: UCH-L5

UCH-L5 in complex with ubiquitin-propargyl bound to the RPN13 DEUBAD domain. Determined by X-ray diffraction at 2.3 Å resolution. Released 4 Mar 2015.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: HOMO SAPIENS
Chains: 3
Atoms: 3,999
Mol. weight: 59.36 kDa
Released: 4 Mar 2015

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

Secondary structure: helices and β-sheets

4UEL contains 31 α-helices and 22 β-strands across 3 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, 12 β-strands

Element	Residues	Length	Sheet
α-helix	9-10	2
β-strand	12	1	1
α-helix	15-25	11
β-strand	28	1	2
β-strand	30-35	6	3
α-helix	41-44	4
β-strand	49-57	9	3
α-helix	62-64	3
β-strand	67-68	2	3
α-helix	69	1
α-helix	72-75	4
α-helix	88-97	10
β-strand	106	1	2
α-helix	108-118	11
α-helix	123-131	9
α-helix	134-141	8
α-helix	144-146	3
β-strand	163-171	9	3
β-strand	174-178	5	3
β-strand	186-190	5	3
β-strand	192	1	4
β-strand	195	1	4
α-helix	197-209	13
β-strand	219-225	7	3
α-helix	227-244	18
α-helix	254-288	35
α-helix	292-304	13
α-helix	308-317	10

Chain B: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	5
β-strand	12-16	5	5
β-strand	22	1	6
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	5
β-strand	48-49	2	5
α-helix	50-51	2
β-strand	55	1	6
α-helix	57-59	3
β-strand	66-71	6	5
β-strand	74	1	1

Chain C: 11 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	288-291	4
α-helix	295-297	3
α-helix	298-301	4
α-helix	304-310	7
α-helix	311-313	3
β-strand	317	1	7
β-strand	320	1	7
α-helix	324-326	3
α-helix	327-331	5
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)
Polyubiquitin-B	B	protein	76	HOMO SAPIENS	P0CG47 (AlphaFold model)
Proteasomal ubiquitin receptor ADRM1	C	protein	127	HOMO SAPIENS	Q16186 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4UEL_1 UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5 (chains A)
GPGMTGNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFK
WQPGEEPAGSVVQDSRLDTIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEF
SQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYE
LDGLREGPIDLGACNQDDWISAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAE
LQRQLAEEPMDTDQGNSMLSAIQSEVAKNQMLIEEEVQKLKRYKIENIRRKHNYLPFIME
LLKTLAEHQQLIPLVEKAKEKQNAKKAQETK

Sequence of entity 2 (B), FASTA

>4UEL_2 POLYUBIQUITIN-B (chains B)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGX

Sequence of entity 3 (C), FASTA

>4UEL_3 PROTEASOMAL UBIQUITIN RECEPTOR ADRM1 (chains C)
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
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…
4UEM 2.82 Å, UCH-L5 in complex with the RPN13 DEUBAD domain
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

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