Research workbench

The structure of the lipid binding protein ce-far-7 from caenorhabditis elegans

Analyse The structure of the lipid binding protein ce-far-7 from caenorhabditis elegans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2W9Y
Type: protein
Length: 136 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fatty ACID/RETINOL binding protein protein 7, isoform a, confirmed by transcript evidence
UniProt: Q9TZ51
Ligands: SO4
Pockets: 1 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 68% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fatty ACID/RETINOL binding protein protein 7, isoform a, confirmed by transcript evidence	protein	136	68% helix, 0% strand	Q9TZ51

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · 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	97	0.53	0.83	27	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

2W9Y · The structure of the lipid binding protein Ce-FAR-7 from Caenorhabditis elegans · the same entry in another collection · chain A against A, 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 Q9TZ51
Elsewhere: RCSB PDB 2W9Y · PDBe 2W9Y · UniProt Q9TZ51

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.