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ForT Mutant T138V

Analyse ForT Mutant T138V in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
8AP0
Type
protein
Length
332 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.6
Source
Streptomyces kaniharaensis
Molecule
Beta-ribofuranosylaminobenzene 5'-phosphate synthase
UniProt
A0A5S9CYM0
Ligands
MYO, PRP, K, MG
Pockets
1 · best druggability 0.78

Structure

x-ray diffraction · resolution 1.6 · 1 distinct chain · 41% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAABeta-ribofuranosylaminobenzene 5'-phosphate synthaseprotein33241% helix, 26% strandA0A5S9CYM0

Ligands and binding sites

  • MYO · 4-azanyl-1~{H}-pyrazole-3,5-dicarboxylic acid · ligand · chains AAA
  • PRP · 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose · sugar · chains AAA
  • K · Potassium ion · metal · chains AAA
  • MG · Magnesium ion · metal · chains AAA
  • GOL · Glycerol · additive · 2 copies · chains AAA

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
14500.780.8747PRP, MYO, MG

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