8EJR: Kelch domain of human KEAP1

Kelch domain of human KEAP1 bound to Nrf2 linear peptide, Ac-GDPETGE-NH2. Determined by X-ray diffraction at 2.08 Å resolution. Released 27 Sept 2023.

Method: X-ray diffraction
Resolution: 2.08 Å
Organism: Homo sapiens
Chains: 3
Atoms: 4,674
Mol. weight: 74.53 kDa
Released: 27 Sept 2023

Explore 8EJR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8EJR contains 10 α-helices and 85 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: 5 helices, 41 β-strands

Element	Residues	Length	Sheet
β-strand	328-331	4	1
β-strand	334	1	2
β-strand	338	1	2
β-strand	342-345	4	1
β-strand	352-354	3	1
α-helix	356-358	3
β-strand	363	1	3
β-strand	366-370	5	4
β-strand	373-377	5	4
β-strand	380-383	4	3
β-strand	386-389	4	3
β-strand	393-397	5	4
β-strand	402-405	4	4
α-helix	407-409	3
β-strand	414	1	5
β-strand	417-421	5	6
β-strand	424-428	5	6
β-strand	431-432	2	5
β-strand	435-436	2	5
β-strand	440-444	5	6
β-strand	449-453	5	6
α-helix	454-456	3
β-strand	461	1	7
β-strand	464-468	5	7
β-strand	471-478	8	7
β-strand	483-491	9	7
β-strand	496-499	4	7
β-strand	501	1	8
α-helix	502-503	2
β-strand	508	1	9
β-strand	511-515	5	10
β-strand	518-522	5	10
β-strand	525	1	9
β-strand	530	1	9
β-strand	534-538	5	10
β-strand	543-547	5	10
α-helix	548-550	3
β-strand	555	1	11
β-strand	558-562	5	12
β-strand	565-569	5	12
β-strand	572	1	11
β-strand	577	1	11
β-strand	580-585	6	12
β-strand	590-596	7	12
β-strand	602	1	2
β-strand	605-608	4	1

Chain B: 5 helices, 44 β-strands

Element	Residues	Length	Sheet
β-strand	328-331	4	13
β-strand	334	1	14
β-strand	338	1	14
β-strand	339	1	15
β-strand	342-345	4	13
β-strand	352-354	3	13
α-helix	356-358	3
β-strand	362	1	15
β-strand	363	1	16
β-strand	366-370	5	17
β-strand	373-377	5	17
β-strand	380-383	4	16
β-strand	386-389	4	16
β-strand	393-397	5	17
β-strand	402-405	4	17
α-helix	407-409	3
β-strand	414	1	18
β-strand	417-421	5	19
β-strand	424-428	5	19
β-strand	431-432	2	18
β-strand	435-436	2	18
β-strand	440-444	5	19
β-strand	449-452	4	19
α-helix	454-456	3
β-strand	461	1	20
β-strand	464-468	5	20
β-strand	471-478	8	20
β-strand	483-491	9	20
β-strand	496-499	4	20
β-strand	501	1	8
α-helix	502-503	2
β-strand	508	1	21
β-strand	511-515	5	22
β-strand	518-522	5	22
β-strand	525	1	21
β-strand	530	1	21
β-strand	534-538	5	22
β-strand	543-546	4	22
α-helix	548-550	3
β-strand	555	1	23
β-strand	558-562	5	24
β-strand	565-569	5	24
β-strand	572	1	23
β-strand	577	1	23
β-strand	581-584	4	24
β-strand	585	1	25
β-strand	590	1	25
β-strand	602	1	14
β-strand	605-608	4	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kelch-like ECH-associated protein 1	A, B	protein	336	Homo sapiens	Q14145 (AlphaFold model)
Linear peptide from Nuclear factor erythroid 2-related factor 2	C	protein	9	Homo sapiens	Q16236 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8EJR_1 Kelch-like ECH-associated protein 1 (chains A, B)
MGSSHHHHHHSSGGENLYFQGHMKPTQVMPSRAPKVGRLIYTAGGYFRQSLSYLEAYNPS
DGTWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAP
MSVPRNRIGVGVIDGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVL
NRLLYAVGGFDGTNRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQ
DQLNSVERYDVATATWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDT
DTWSEVTRMTSGRSGVGVAVTMEPSRKQIDQQNSTS

Sequence of entity 2 (C), FASTA

>8EJR_2 Linear peptide from Nuclear factor erythroid 2-related factor 2 (chains C)
XGDPETGEX

Primary citation

The benefit of cyclization: a comparison of cyclic and linear peptide inhibitors of the KEAP1/Nrf2 protein-protein interaction. Muellers, S.N., Allen, K.N., Whitty, A. To be published.

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

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