5NLB: Human CUL3 N-terminal domain

Crystal structure of human CUL3 N-terminal domain bound to KEAP1 BTB and 3-box. Determined by X-ray diffraction at 3.45 Å resolution. Released 19 Apr 2017.

Method: X-ray diffraction
Resolution: 3.45 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,882
Mol. weight: 58.9 kDa
Released: 19 Apr 2017

Explore 5NLB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5NLB contains 35 α-helices and 3 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, 3 β-strands

Element	Residues	Length	Sheet
α-helix	58-72	15
β-strand	79-83	5	1
α-helix	89-90	2
β-strand	91-95	5	1
α-helix	97-103	7
α-helix	105-110	6
β-strand	123-125	3	1
α-helix	130-142	13
α-helix	152-162	11
α-helix	165-172	8
α-helix	184-194	11
α-helix	199-202	4

Chain B: 26 helices, 0 β-strands

Element	Residues	Length
α-helix	27-45	19
α-helix	54-66	13
α-helix	70-84	15
α-helix	85-90	6
α-helix	91-94	4
α-helix	101-122	22
α-helix	124-133	10
α-helix	139-147	9
α-helix	148-152	5
α-helix	156-173	18
α-helix	180-192	13
α-helix	199-201	3
α-helix	202-206	5
α-helix	207-226	20
α-helix	230-250	21
α-helix	254-256	3
α-helix	257-264	8
α-helix	265-269	5
α-helix	270-272	3
α-helix	273-277	5
α-helix	284-289	6
α-helix	293-303	11
α-helix	309-329	21
α-helix	340-354	15
α-helix	355-359	5
α-helix	364-380	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kelch-like ECH-associated protein 1	A	protein	154	Homo sapiens	Q14145 (AlphaFold model)
Cullin-3	B	protein	356	Homo sapiens	Q13618 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5NLB_1 Kelch-like ECH-associated protein 1 (chains A)
TFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAM
FTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRA
CSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAR

Sequence of entity 2 (B), FASTA

>5NLB_2 Cullin-3 (chains B)
DEKYVNSIWDLLKNAIQEIQRKNNSGLSFEELYRNAYTMVLHKHGEKLYTGLREVVTEHL
INKVREDVLNSLNNNFLQTLNQAWNDHQTAMVMIRDILMYMDRVYVQQNNVENVYNLGLI
IFRDQVVRYGCIRDHLRQTLLDMIARERKGEVVDRGAIRNACQMLMILGLEGRSVYEEDF
EAPFLEMSAEFFQMESQKFLAENSASVYIKKVEARINEEIERVMHCLDKSTEEPIVKVVE
RELISKHMKTIVEMENSGLVHMLKNGKTEDLGCMYKLFSRVPNGLKTMCECMSSYLREQG
KALVSEEGEGKNPVDYRQGLDDLKSRFDRFLLESFNNDRLFKQTIAGDFEYFLNLN

Primary citation

Structural and biochemical characterization establishes a detailed understanding of KEAP1-CUL3 complex assembly. Adamson, R.J., Payne, N.C., Bartual, S.G. et al. Free Radic Biol Med (2023) 204:215-225. DOI 10.1016/j.freeradbiomed.2023.04.021 · PubMed

Other PDB entries of the same protein (UniProt Q14145 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8XGK 1.32 Å, Optimization Efforts for Identification of Novel Highly Potent Keap1-Nrf2…
1ZGK 1.35 Å, 1.35 angstrom structure of the Kelch domain of Keap1
8XGV 1.42 Å, Optimization Efforts for Identification of Novel Highly Potent Keap1-Nrf2…
6TYM 1.42 Å, KEAP1 Kelch domain in complex with Compound 9
9KVW 1.44 Å, Crystal Structures of Keap1-compound complexes
8IXS 1.48 Å, Methyl and Fluorine Effects in Novel Orally Bioavailable Keap1/Nrf2 PPI Inhibitor for…
2FLU 1.5 Å, Crystal Structure of the Kelch-Neh2 Complex
8IVR 1.5 Å, Methyl and Fluorine Effects in Novel Orally Bioavailable Keap1/Nrf2 PPI Inhibitor for…
9R1Z 1.5 Å, Keap1 - inhibitor complex - 3
8PKW 1.54 Å, Kelch domain of KEAP1 in complex with a ortho-dimethylbenzene linked cyclic peptide 5…
8PKV 1.55 Å, Kelch domain of KEAP1 in complex with a ortho-dimethylbenzene linked cyclic peptide 4…
9M24 1.57 Å, Crystal Structure of kelch domain of human KEAP1 in complex with CH7450924

Browse structure collections

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