MolNFT v1 · #183486 · protein

Conformation 1 of straight filament from primary age-related tauopathy brain

7NRS · Microtubule-associated protein tau: “Conformation 1 of straight filament from primary age-related tauopathy brain”. Electron microscopy, 2 pockets (best druggability 0.51). MolNFT v1 #183486 on GenesisL1: 3D structure, binding sites…

PDB: 7NRS
Type: protein
Length: 770 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 2 · best druggability 0.51

Structure

electron microscopy · 1 distinct chain · 0% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, I, B, D, F, H, C, E, G, J	Microtubule-associated protein tau	protein	77	0% helix, 58% strand	P10636

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	196	0.51	0.77	33	empty
2	155	0.41	0.73	27	empty

Interfaces

17 interfaces between chains.

C–E · 3192 Å² buried · 101 hydrogen bonds · protein-protein
I–G · 3191 Å² buried · 101 hydrogen bonds · protein-protein
G–J · 3191 Å² buried · 101 hydrogen bonds · protein-protein
I–C · 3191 Å² buried · 100 hydrogen bonds · protein-protein
A–F · 3183 Å² buried · 99 hydrogen bonds · protein-protein

Compared structures

7NRS · Conformation 1 of straight filament from primary age-related tauopathy brain · the same entry in another collection · chain G against G, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P10636
Elsewhere: RCSB PDB 7NRS · PDBe 7NRS · UniProt P10636

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