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Cryo-EM structure of ATNBR1-PB1 filament (S-type)

Analyse Cryo-EM structure of ATNBR1-PB1 filament (S-type) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6TGP
Type: protein
Length: 176 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein NBR1 homolog
UniProt: Q9SB64
Pockets: 1 · best druggability 0.37

Structure

electron microscopy · 1 distinct chain · 18% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein NBR1 homolog	protein	88	18% helix, 28% strand	Q9SB64

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	88	0.37	0.76	14	empty

Interfaces

1 interface between chains.

A–B · 338 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

6TGP · Cryo-EM structure of AtNBR1-PB1 filament (S-type) · the same entry in another collection · chain A against A, TM-score 1.00
Q9SB64 · AlphaFold monomer V2.0 prediction for protein NBR1 homolog (Q9SB64) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q9SB64
Elsewhere: RCSB PDB 6TGP · PDBe 6TGP · UniProt Q9SB64

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