4UF5: UCH-L5

Crystal structure of UCH-L5 in complex with inhibitory fragment of INO80G. Determined by X-ray diffraction at 3.7 Å resolution. Released 4 Mar 2015.

Method: X-ray diffraction
Resolution: 3.7 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 3,296
Mol. weight: 53.5 kDa
Released: 4 Mar 2015

Explore 4UF5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4UF5 contains 19 α-helices and 9 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: 14 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	15-24	10
β-strand	28	1	1
β-strand	30-34	5	2
α-helix	40-44	5
α-helix	47	1
β-strand	49-56	8	2
β-strand	68	1	2
α-helix	73-76	4
α-helix	88-97	10
β-strand	106	1	1
α-helix	109-117	9
α-helix	123-132	10
α-helix	134-145	12
β-strand	164-171	8	2
β-strand	174-179	6	2
β-strand	186-190	5	2
α-helix	197-214	18
β-strand	218-225	8	2
α-helix	227-231	5
α-helix	234-242	9
α-helix	256-288	33
α-helix	292-304	13
α-helix	308-319	12

Chain B: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	48-60	13
α-helix	64-73	10
α-helix	81-93	13
α-helix	103-112	10
α-helix	118-152	35

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin carboxyl-terminal hydrolase isozyme L5	A	protein	331	HOMO SAPIENS	Q9Y5K5 (AlphaFold model)
Nuclear factor related to kappa-B-binding protein	B	protein	134	HOMO SAPIENS	Q6P4R8 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4UF5_1 UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5 (chains A)
GPGMTGNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPENFEKLKPVHGLIFLFK
WQPGEEPAGSVVQDSRLDTIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEF
SQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTSAKEEDAFHFVSYVPVNGRLYE
LDGLREGPIDLGACNQDDWISAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAE
LQRQLAEEPMDTDQGNSMLSAIQSEVAKNQMLIEEEVQKLKRYKIENIRRKHNYLPFIME
LLKTLAEHQQLIPLVEKAKEKQNAKKAQETK

Sequence of entity 2 (B), FASTA

>4UF5_2 NUCLEAR FACTOR RELATED TO KAPPA-B-BINDING PROTEIN (chains B)
GPGEDLLEDPEIFFDVVSLSTWQEVLSDSQREHLQQFLPQFPEDSAEQQNELILALFSGE
NFRFGNPLHIAQKLFRDGHFNPEVVKYRQLCFKSQYKRYLNSQQQYFHRLLKQILASRSD
LLEMARRSGPALPF

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…
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

Browse structure collections

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