1ZGK: Kelch-like ECH-associated protein 1

1.35 angstrom structure of the Kelch domain of Keap1. Determined by X-ray diffraction at 1.35 Å resolution. Released 4 Oct 2005.

Method: X-ray diffraction
Resolution: 1.35 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,651
Mol. weight: 34.02 kDa
Released: 4 Oct 2005

Explore 1ZGK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ZGK contains 5 α-helices and 42 β-strands across 1 chain. 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, 42 β-strands

Element	Residues	Length	Sheet
β-strand	328-331	4	1
β-strand	334-335	2	2
β-strand	337-338	2	2
β-strand	342-346	5	1
β-strand	351-354	4	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	449-452	4	6
α-helix	454-456	3
β-strand	461	1	7
β-strand	464-468	5	8
β-strand	471-475	5	8
β-strand	478	1	7
β-strand	483	1	7
β-strand	487-491	5	8
β-strand	496-499	4	8
α-helix	501-503	3
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	543-546	4	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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kelch-like ECH-associated protein 1	A	protein	308	Homo sapiens	Q14145 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1ZGK_1 Kelch-like ECH-associated protein 1 (chains A)
GSSHHHHHHSSGLVPRGSHAPKVGRLIYTAGGYFRQSLSYLEAYNPSNGTWLRLADLQVP
RSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAPMSVPRNRIGVGVI
DGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGT
NRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVET
ETWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDTDTWSEVTRMTSGR
SGVGVAVT

Primary citation

Conserved solvent and side-chain interactions in the 1.35 Angstrom structure of the Kelch domain of Keap1. Beamer, L.J., Li, X., Bottoms, C.A. et al. Acta Crystallogr D Biol Crystallogr (2005) 61:1335-1342. DOI 10.1107/S0907444905022626 · 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…
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
6V6Z 1.6 Å, Crystal structure of N-[(4-methoxyphenyl)sulfonyl]-N-(4-{[(4-methoxyphenyl)sulfonyl]amino…

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