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Solution NMR structure of farnesylated PEX19, C-terminal domain

Analyse Solution NMR structure of farnesylated PEX19, C-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LNF
Type: protein
Length: 139 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peroxisomal biogenesis factor 19
UniProt: P40855
Ligands: FAR
Pockets: 3 · best druggability 0.80

Structure

solution nmr · 1 distinct chain · 58% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peroxisomal biogenesis factor 19	protein	139	58% helix, 0% strand	P40855

Ligands and binding sites

FAR · Farnesyl · ligand · chains A

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

Pockets

3 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	138	0.80	0.96	20	FAR
2	73	0.42	0.80	15	empty
3	87	0.36	0.75	17	empty

Modifications

Observed in the structure: 1 lipid (farnesylation).

Compared structures

5LNF · Solution NMR structure of farnesylated PEX19, C-terminal domain · the same entry in another collection · chain A against A, TM-score 1.00
P40855 · AlphaFold monomer V2.0 prediction for peroxisomal biogenesis factor 19 (P40855) · a predicted model of the same protein · chain A against A, TM-score 0.70

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 P40855
Elsewhere: RCSB PDB 5LNF · PDBe 5LNF · UniProt P40855

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