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Mycobacterium smegmatis flap endonuclease mutant D208N

Analyse Mycobacterium smegmatis flap endonuclease mutant D208N in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6C36
Type
protein
Length
317 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
5'-3' exonuclease
UniProt
I7GAS0
Ligands
MN, PO4
Pockets
3 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A5'-3' exonucleaseprotein31749% helix, 12% strandI7GAS0

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 3 copies · chains A
  • PO4 · Phosphate ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14040.610.7741MN, PO4
2680.370.7714empty
3840.340.7521empty

Compared structures

  • 6C36 · Mycobacterium smegmatis flap endonuclease mutant D208N · the same entry in another collection · chain A against A, TM-score 1.00

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