9B3N: Human Notch-1 EGFs 20-24

Human Notch-1 EGFs 20-24. Determined by X-ray diffraction at 1.5 Å resolution. Released 16 Oct 2024.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,810
Mol. weight: 22.85 kDa
Ligands: BGC, FUC, CA
Released: 16 Oct 2024

Explore 9B3N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9B3N contains 10 α-helices and 20 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: 10 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	756-759	4
β-strand	767-771	5	1
β-strand	774-778	5	1
α-helix	779-780	2
β-strand	783-784	2	2
β-strand	790-791	2	2
α-helix	794-797	4
β-strand	805-809	5	3
β-strand	812-816	5	3
α-helix	817-818	2
β-strand	821-822	2	4
β-strand	828-829	2	4
α-helix	842	1
β-strand	843-846	4	5
β-strand	853-856	4	5
α-helix	857-858	2
β-strand	861-862	2	6
β-strand	868-869	2	6
α-helix	872-875	4
α-helix	882	1
β-strand	883-887	5	7
β-strand	890-894	5	7
α-helix	895-896	2
β-strand	899-900	2	8
β-strand	906-907	2	8
β-strand	921-925	5	9
β-strand	928-932	5	9
α-helix	933-934	2
β-strand	937-938	2	10
β-strand	944-945	2	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Neurogenic locus notch homolog protein 1	A	protein	201	Homo sapiens	P46531 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9B3N_1 Neurogenic locus notch homolog protein 1 (chains A)
NNNECESNPCVNGGTCKDMTSGYVCTCREGFSGPNCQTNINECASNPCLNQGTCIDDVAG
YKCNCLLPYTGATCEVVLAPCAPSPCRNGGECRQSEDYESFSCVCPTGWQGQTCEVDINE
CVLSPCRHGASCQNTHGGYRCHCQAGYSGRNCETDIDDCRPNPCHNGGSCTDGINTAFCD
CLPGFRGTFCEEGSGLEVLFQ

Ligands and cofactors

ID	Name	Formula	Copies
BGC	beta-D-glucopyranose	C6 H12 O6	1
FUC	alpha-L-fucopyranose	C6 H12 O5	4
CA	Calcium ion	Ca	4

Water and common crystallization additives (EDO) are not listed.

Primary citation

Structural and functional studies of the EGF20-27 region reveal new features of the human Notch receptor important for optimal activation. Bo, Z., Rowntree, T., Johnson, S. et al. Structure (2024) 32:2325-2336.e5. DOI 10.1016/j.str.2024.10.012 · PubMed

Other PDB entries of the same protein (UniProt P46531 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5L0R 1.5 Å, human POGLUT1 in complex with Notch1 EGF12 and UDP
2F8Y 1.55 Å, Crystal structure of human Notch1 ankyrin repeats to 1.55A resolution.
9B3G 1.55 Å, Human Notch-1 EGFs 21-23
4D0E 1.61 Å, Human Notch1 EGF domains 11-13 mutant GlcNAc-fucose disaccharide modified at T466
4CUD 1.85 Å, Human Notch1 EGF domains 11-13 mutant fucosylated at T466
2HE0 1.9 Å, Crystal structure of a human Notch1 ankyrin domain mutant
1YYH 1.9 Å, Crystal structure of the human Notch 1 ankyrin domain
3ETO 2.0 Å, 2 Angstrom Xray structure of the NOTCH1 Negative Regulatory Region (NRR)
5UB5 2.09 Å, human POGLUT1 in complex with human Notch1 EGF12 S458T mutant and UDP
3L95 2.19 Å, Crystal structure of the human Notch1 Negative Regulatory Region (NRR) bound to the fab…
4CUF 2.29 Å, Human Notch1 EGF domains 11-13 mutant T466S
5FMA 2.46 Å, human Notch 1, EGF 4-7

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