GL1X · GenesisL1 explorer

MolNFT v1 · #157325 · protein

Crystal structure of FMN-binding beta-glucuronidase from facaelibacterium prausnitzii L2-6

6MVF · Beta-GALACTOSIDASE/BETA-glucuronidase: “Crystal structure of FMN-binding beta-glucuronidase from facaelibacterium prausnitzii L2-6”. X-ray diffraction, 1 ligand (FMN), 20 pockets (best druggability 0.70). MolNFT v1 #157325 on…

PDB
6MVF
Type
protein
Length
3,858 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-GALACTOSIDASE/BETA-glucuronidase
EC
3.2.1.23
UniProt
D4K3H3
Ligands
FMN
Pockets
20 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FBeta-GALACTOSIDASE/BETA-glucuronidase (EC 3.2.1.23)protein64317% helix, 38% strandD4K3H3

Ligands and binding sites

  • FMN · Flavin mononucleotide · ligand · 6 copies · chains A, B, C, D, E, F

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14790.700.8146empty
24750.690.8048empty
37810.690.7685empty
44770.690.8048empty
54450.680.8043empty

Interfaces

9 interfaces between chains.

  • B–E · 1245 Ų buried · 25 hydrogen bonds · protein-protein
  • A–F · 1243 Ų buried · 23 hydrogen bonds · protein-protein
  • A–C · 1243 Ų buried · 21 hydrogen bonds · protein-protein
  • C–F · 1242 Ų buried · 23 hydrogen bonds · protein-protein
  • D–E · 1235 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

  • 6MVF · Crystal structure of FMN-binding beta-glucuronidase from Facaelibacterium prausnitzii L2-6 · 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.