MolNFT v1 · #64281 · protein

Crystal structure of degv, a fatty acid binding protein from bacillus subtilis

3FYS · Protein degv: “Crystal structure of degv, a fatty acid binding protein from bacillus subtilis”. X-ray diffraction, 2 ligands (PLM, BR), 2 pockets (best druggability 0.76). MolNFT v1 #64281 on GenesisL1: 3D structure, binding sites…

PDB: 3FYS
Type: protein
Length: 282 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein degv
UniProt: P32436
Ligands: PLM, BR
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein degv	protein	282	42% helix, 26% strand	P32436

Ligands and binding sites

PLM · Palmitic acid · ligand · chains A
BR · Bromide ion · ion · 7 copies · chains A
EDO · 1,2-ethanediol · additive · chains A

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

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	123	0.76	0.95	29	PLM
2	79	0.40	0.78	14	EDO

Compared structures

3FYS · Crystal Structure of DegV, a fatty acid binding protein from Bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
P32436 · AlphaFold monomer V2.0 prediction for protein degv (P32436) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P32436
Elsewhere: RCSB PDB 3FYS · PDBe 3FYS · UniProt P32436

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