3ETO: Neurogenic locus notch homolog protein 1

2 Angstrom Xray structure of the NOTCH1 Negative Regulatory Region (NRR). Determined by X-ray diffraction at 2.0 Å resolution. Released 23 Dec 2008.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,884
Mol. weight: 54.54 kDa
Ligands: CA
Released: 23 Dec 2008

Explore 3ETO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3ETO contains 34 α-helices and 20 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: 17 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	1453-1458	6
α-helix	1466-1468	3
α-helix	1471-1473	3
α-helix	1474-1477	4
α-helix	1493-1495	3
α-helix	1497-1499	3
α-helix	1508-1510	3
α-helix	1513-1520	8
α-helix	1524-1525	2
α-helix	1534-1540	7
α-helix	1548-1550	3
α-helix	1553-1560	8
β-strand	1570	1	1
α-helix	1571	1
β-strand	1572	1	2
β-strand	1574-1579	6	1
α-helix	1583-1588	6
α-helix	1590-1601	12
β-strand	1604-1607	4	1
β-strand	1609	1	3
β-strand	1615	1	3
β-strand	1617-1621	5	1
β-strand	1673-1682	10	1
α-helix	1686-1689	4
β-strand	1696	1	2
α-helix	1697-1710	14
β-strand	1719-1725	7	1

Chain B: 17 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	1453-1458	6
α-helix	1466-1468	3
α-helix	1471-1473	3
α-helix	1474-1477	4
α-helix	1493-1495	3
α-helix	1497-1499	3
α-helix	1508-1510	3
α-helix	1513-1520	8
α-helix	1524-1525	2
α-helix	1534-1539	6
α-helix	1548-1550	3
α-helix	1556-1560	5
β-strand	1570	1	4
α-helix	1571	1
β-strand	1572	1	5
β-strand	1574-1579	6	4
α-helix	1583-1587	5
α-helix	1590-1601	12
β-strand	1604-1607	4	4
β-strand	1609	1	6
β-strand	1615	1	6
β-strand	1617-1621	5	4
β-strand	1673-1682	10	4
α-helix	1686-1689	4
β-strand	1696	1	5
α-helix	1697-1710	14
β-strand	1719-1725	7	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Neurogenic locus notch homolog protein 1	A, B	protein	242	Homo sapiens	P46531 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3ETO_1 Neurogenic locus notch homolog protein 1 (chains A, B)
GEEACELPECQEDAGNKVCSLQCNNHACGWDGGDCSLNFNDPWKNCTQSLQCWKYFSDGH
CDSQCNSAGCLFDGFDCQRAEGQCNPLYDQYCKDHFSDGHCDQGCNSAECEWDGLDCAEH
VPERLAAGTLVVVVLMPPEQLRNSSFHFLRELSRVLHTNVVFKRDAHGQQMIFPYYGMDV
RGSIVYLEIDNRQCVQASSQCFQSATDVAAFLGALASLGSLNIPYKIEAVQSETVEPPPP
AQ

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	6

Water and common crystallization additives (CL, GOL) are not listed.

Primary citation

Structure of the Notch1-negative regulatory region: implications for normal activation and pathogenic signaling in T-ALL. Gordon, W.R., Roy, M., Vardar-Ulu, D. et al. Blood (2009) 113:4381-4390. DOI 10.1182/blood-2008-08-174748 · 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
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
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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