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Structure of B. megaterium NFRA1

Analyse Structure of B. megaterium NFRA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5HDJ
Type
protein
Length
495 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NFRA1
UniProt
A0A0K0VJM9
Ligands
FMN
Pockets
6 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANFRA1protein24753% helix, 14% strandA0A0K0VJM9
BNFRA1protein24852% helix, 14% strandA0A0K0VJM9

Ligands and binding sites

  • FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 3 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14030.670.8044FMN
23990.650.7944FMN, EDO
3670.340.7616empty
4710.310.7414empty
5580.300.7615empty

Interfaces

1 interface between chains.

  • A–B · 5251 Ų buried · 75 hydrogen bonds · protein-protein

Compared structures

  • 5HDJ · Structure of B. megaterium NfrA1 · the same entry in another collection · chain A against A, TM-score 1.00

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