GL1X · GenesisL1 explorer

Research workbench

The crystal structure of a flavoprotein from sinorhizobium meliloti

Analyse The crystal structure of a flavoprotein from sinorhizobium meliloti in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3V76
Type
protein
Length
390 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Flavoprotein
UniProt
Q92RY0
Ligands
FDA
Pockets
2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFlavoproteinprotein39037% helix, 27% strandQ92RY0

Ligands and binding sites

  • FDA · Dihydroflavine-adenine dinucleotide · ligand · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14490.770.8561FDA
2550.360.7915empty

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

  • 3V76 · The crystal structure of a flavoprotein from Sinorhizobium meliloti · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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