6NWP: Microtubule-associated protein tau

Chronic traumatic encephalopathy Type I Tau filament. Determined by electron microscopy at 2.3 Å resolution. Released 27 Mar 2019.

Method: Electron microscopy
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 6
Atoms: 3,792
Mol. weight: 275.52 kDa
Released: 27 Mar 2019

Explore 6NWP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6NWP contains 0 α-helices and 49 β-strands across 6 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.

Chains A, B, C, D and F: 0 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	306-310	5	1
β-strand	313-314	2	2
β-strand	317-322	6	3
β-strand	325-330	6	4
β-strand	337-346	10	5
β-strand	350-357	8	6
β-strand	360-362	3	7
β-strand	369-378	10	8

Chain E: 0 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	307-310	4	1
β-strand	313-314	2	2
β-strand	317-322	6	3
β-strand	325-330	6	4
β-strand	337-342	6	5
β-strand	345-346	2	5
β-strand	350-357	8	6
β-strand	360-362	3	7
β-strand	369-378	10	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Microtubule-associated protein tau	A, B, C, D, E, F	protein	441	Homo sapiens	P10636 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>6NWP_1 Microtubule-associated protein tau (chains A, B, C, D, E, F)
MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPG
SETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAG
HVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPK
TPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAK
SRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHV
PGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNI
THVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMV
DSPQLATLADEVSASLAKQGL

Primary citation

Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules. Falcon, B., Zivanov, J., Zhang, W. et al. Nature (2019) 568:420-423. DOI 10.1038/s41586-019-1026-5 · PubMed

Other PDB entries of the same protein (UniProt P10636 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6ODG 1.0 Å, SVQIVY, Crystal Structure of a tau protein fragment
8KDX 1.01 Å, Tau-S214 Phosphorylation Inhibits Fyn Kinase Interaction and Increases the Decay Time of…
5K7N 1.1 Å, MicroED structure of tau VQIVYK peptide at 1.1 A resolution
9GG8 1.1 Å, Crystal structure of 14-3-3 sigma dC - C38N in complex with Tau pS214 peptide and…
9GG7 1.24 Å, Crystal structure of 14-3-3 sigma dC - C38N in complex with Tau pS324 peptide and…
5V5C 1.25 Å, VQIINK, Structure of the amyloid-spine from microtubule associated protein tau Repeat 2
6FAU 1.25 Å, Crystal structure of C-terminal modified Tau peptide-hybrid 4.2e-I with 14-3-3sigma
8GCK 1.37 Å, Crystal structure of the human CHIP-TPR domain in complex with a 6mer acetylated tau…
4Y5I 1.4 Å, Crystal structure of C-terminal modified Tau peptide-hybrid 126B with 14-3-3sigma
6FAV 1.4 Å, Crystal structure of C-terminal modified Tau peptide-hybrid 4.2f-I with 14-3-3sigma
6FAW 1.4 Å, Crystal structure of C-terminal modified Tau peptide-hybrid 4.2c-I with 14-3-3sigma
9GHK 1.42 Å, Crystal structure of Fyn SH3 domain/tau 214-220 peptide complex

Browse more

6NWP is part of these collections:

Protein folding, misfolding and amyloid

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