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Solution structure of the epsilon subunit of the F1-atpsynthase from escherichia COLI and orientation of the subunit relative to the beta subunits of the complex

Analyse Solution structure of the epsilon subunit of the F1-atpsynthase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BSH
Type: protein
Length: 138 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (epsilon subunit)
EC: 3.6.1.34
UniProt: P0A6E6
Pockets: 2 · best druggability 0.61

Structure

solution nmr · 1 distinct chain · 21% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (epsilon subunit) (EC 3.6.1.34)	protein	138	21% helix, 28% strand	P0A6E6

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	117	0.61	0.86	27	empty
2	91	0.35	0.74	21	empty

Compared structures

1BSH · Solution structure of the epsilon subunit of the F1-atpsynthase from escherichia COLI and… · the same entry in another collection · chain A against A, TM-score 1.00
P0A6E6 · AlphaFold monomer V2.0 prediction for ATP synthase epsilon chain (P0A6E6) · a predicted model of the same protein · chain A against A, TM-score 0.84

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 P0A6E6
Elsewhere: RCSB PDB 1BSH · PDBe 1BSH · UniProt P0A6E6

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