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Ppta from streptomyces chartreusis

Analyse Ppta from streptomyces chartreusis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6RN5
Type
protein
Length
283 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chad domain protein
UniProt
A0A2N9BBV4
Ligands
CU, SO4, CL, CO3
Pockets
4 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 79% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChad domain proteinprotein28379% helix, 1% strandA0A2N9BBV4

Ligands and binding sites

  • CU · Copper (II) ion · metal · 2 copies · chains A
  • SO4 · Sulfate ion · ion · 4 copies · chains A
  • CL · Chloride ion · ion · 2 copies · chains A
  • CO3 · Carbonate ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13590.590.7640SO4
2860.400.7817empty
3560.300.7514CL
4610.280.7413empty

Compared structures

  • 6RN5 · PptA from Streptomyces chartreusis · the same entry in another collection · chain A against A, TM-score 1.00

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