5FMA: Human Notch 1, EGF 4-7

human Notch 1, EGF 4-7. Determined by X-ray diffraction at 2.46 Å resolution. Released 13 Apr 2016.

Method: X-ray diffraction
Resolution: 2.46 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 2,254
Mol. weight: 33.16 kDa
Ligands: CA
Released: 13 Apr 2016

Explore 5FMA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5FMA contains 19 α-helices and 28 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: 10 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	143-146	4
α-helix	153	1
β-strand	154-157	4	1
β-strand	162-165	4	1
β-strand	170-171	2	2
β-strand	177-178	2	2
α-helix	179	1
α-helix	181-184	4
α-helix	193	1
β-strand	194-198	5	3
β-strand	201-205	5	3
β-strand	210-211	2	4
β-strand	217-218	2	4
α-helix	219	1
α-helix	231	1
β-strand	232-235	4	5
β-strand	241-244	4	5
α-helix	245-246	2
β-strand	249-250	2	6
β-strand	256-257	2	6
α-helix	258-259	2
α-helix	270	1
β-strand	271-274	4	7
β-strand	279-282	4	7

Chain B: 9 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	143-146	4
β-strand	154-156	3	8
β-strand	163-165	3	8
β-strand	170-171	2	9
β-strand	177-178	2	9
α-helix	179	1
α-helix	181-184	4
α-helix	193	1
β-strand	194-198	5	10
β-strand	201-205	5	10
β-strand	210-211	2	11
β-strand	217-218	2	11
α-helix	219	1
α-helix	231	1
β-strand	232-235	4	12
β-strand	241-244	4	12
α-helix	245-246	2
β-strand	249-250	2	13
β-strand	256-257	2	13
α-helix	258-259	2
α-helix	270	1
β-strand	271-274	4	14
β-strand	279-282	4	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Neurogenic locus notch homolog protein 1	A, B	protein	154	HOMO SAPIENS	P46531 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5FMA_1 NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1 (chains A, B)
QDPCASNPCANGGQCLPFEASYICHCPPSFHGPTCRQDVNECGEKPGLCRHGGTCHNEVG
SYRCVCRATHTGPNCERPYVPCSPSPCQNGGTCRPTGDVTHECACLPGFTGQNCEENIDD
CPGNNCKNGGACVDGVNTYNCRCPPEWTGQYCTE

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	5

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

Primary citation

Non-Linear and Flexible Regions of the Human Notch1 Extracellular Domain Revealed by High-Resolution Structural Studies. Weisshuhn, P.C., Sheppard, D., Taylor, P. et al. Structure (2016) 24:555. DOI 10.1016/J.STR.2016.02.010 · 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
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

Browse structure collections

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