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The ternary complex of prnb (the second enzyme in pyrrolnitrin biosynthesis pathway), tryptophan and cyanide

Analyse The ternary complex of prnb (the second enzyme in pyrrolnitrin biosynthesis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2X67
Type
protein
Length
350 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Prnb
UniProt
P95481
Ligands
HEM, TRP, SO4, CYN
Pockets
2 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 68% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APrnbprotein35068% helix, 2% strandP95481

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · chains A
  • TRP · Tryptophan · ligand · chains A
  • SO4 · Sulfate ion · ion · 2 copies · chains A
  • CYN · Cyanide ion · ion · 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
14500.870.9452HEM, TRP, CYN
2550.280.7417empty

Compared structures

  • 2X67 · The ternary complex of PrnB (the second enzyme in pyrrolnitrin biosynthesis pathway)… · the same entry in another collection · chain A against A, TM-score 1.00
  • P95481 · AlphaFold monomer V2.0 prediction for monodechloroaminopyrrolnitrin synthase prnb (P95481) · a predicted model of the same protein · chain A against A, TM-score 1.00

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