2F8Y: Human Notch1 ankyrin repeats to 1.55A resolution

Name: PDB 2F8Y: Crystal structure of human Notch1 ankyrin repeats to 1.55A resolution.
Published: 2006-04-04
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transcription

Crystal structure of human Notch1 ankyrin repeats to 1.55A resolution. Determined by X-ray diffraction at 1.55 Å resolution. Released 4 Apr 2006.

Method: X-ray diffraction
Resolution: 1.55 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,695
Mol. weight: 49.2 kDa
Released: 4 Apr 2006

Explore 2F8Y in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2F8Y contains 25 α-helices and 6 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: 12 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	1911-1912	2	1
β-strand	1915-1916	2	1
α-helix	1932-1938	7
α-helix	1942-1950	9
α-helix	1965-1971	7
α-helix	1975-1983	9
β-strand	1984	1	2
α-helix	1999-2006	8
α-helix	2009-2017	9
β-strand	2025	1	3
β-strand	2031	1	3
α-helix	2032-2038	7
α-helix	2042-2050	9
α-helix	2065-2072	8
α-helix	2075-2083	9
α-helix	2098-2104	7
α-helix	2108-2116	9

Chain B: 13 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	1913-1916	4
α-helix	1932-1938	7
α-helix	1942-1950	9
α-helix	1965-1972	8
α-helix	1975-1982	8
β-strand	1984	1	2
α-helix	1999-2006	8
α-helix	2009-2017	9
α-helix	2032-2038	7
α-helix	2042-2050	9
α-helix	2065-2072	8
α-helix	2075-2083	9
α-helix	2098-2104	7
α-helix	2108-2116	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Notch homolog 1, translocation-associated (Drosophila)	A, B	protein	223	Homo sapiens	P46531 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2F8Y_1 Notch homolog 1, translocation-associated (Drosophila) (chains A, B)
GDAPAVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRT
PLHAAVSADAQGVFQILIRNRATDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNA
VDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGSYETAKVLLDH
FANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNLVRSPQLHG

Primary citation

Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes. Nam, Y., Sliz, P., Song, L. et al. Cell (2006) 124:973-983. DOI 10.1016/j.cell.2005.12.037 · 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
9B3N 1.5 Å, Human Notch-1 EGFs 20-24
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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