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Crystal structure of ATP synthase epsion chain ATP synthase epsilon chain (ATP synthase F1 sector epsilon subunit) (F-ATPase epsilon subunit) from mycobacterium smegmatis

Analyse Crystal structure of ATP synthase epsion chain ATP synthase epsilon chain (ATP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6PI4
Type: protein
Length: 119 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP synthase epsilon chain
UniProt: A0R1Z9
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATP synthase epsilon chain	protein	119	18% helix, 33% strand	A0R1Z9

Ligands and binding sites

CAC · Cacodylate ion · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	302	0.64	0.80	37	empty

Compared structures

6PI4 · Crystal structure of ATP synthase epsion chain ATP synthase epsilon chain (ATP synthase… · the same entry in another collection · chain A against A, TM-score 1.00
A0R1Z9 · AlphaFold monomer V2.0 prediction for ATP synthase epsilon chain (A0R1Z9) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 A0R1Z9
Elsewhere: RCSB PDB 6PI4 · PDBe 6PI4 · UniProt A0R1Z9

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