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Rifr - type II thioesterase from rifamycin NRPS/PKS biosynthetic pathway - form 2

Analyse Rifr - type II thioesterase from rifamycin NRPS/PKS biosynthetic pathway - form… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3FLB
Type
protein
Length
245 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rifr
EC
3.1.2.-
UniProt
Q7BUF9
Ligands
CL
Pockets
1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARifr (EC 3.1.2.-)protein24547% helix, 16% strandQ7BUF9

Ligands and binding sites

  • CL · Chloride ion · ion · chains A
  • PG4 · Tetraethylene glycol · additive · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1880.540.8414PG4

Compared structures

  • 3FLB · RifR - Type II thioesterase from Rifamycin NRPS/PKS biosynthetic pathway - Form 2 · the same entry in another collection · chain A against A, TM-score 1.00

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