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X-ray structure of the endo-beta-1,4-mannanase from thermotoga petrophila

Analyse X-ray structure of the endo-beta-1,4-mannanase from thermotoga petrophila in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6TN6
Type
protein
Length
465 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mannan endo-1,4-beta-mannosidase. glycosyl hydrolase family 5
EC
3.2.1.78
UniProt
A5IMX7
Ligands
NA, CO3, CL
Pockets
3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMannan endo-1,4-beta-mannosidase. glycosyl hydrolase family 5 (EC 3.2.1.78)protein46533% helix, 26% strandA5IMX7

Ligands and binding sites

  • NA · Sodium ion · metal · chains A
  • CO3 · Carbonate ion · ion · 2 copies · chains A
  • CL · Chloride ion · ion · chains A
  • EDO · 1,2-ethanediol · additive · 9 copies · chains A
  • MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A
  • ACT · Acetate ion · additive · chains A
  • GOL · Glycerol · additive · chains A
  • PEG · Di(hydroxyethyl)ether · additive · chains A
  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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
1820.510.8314ACT
21590.460.7626CO3, TRS
3750.340.7516empty

Compared structures

  • 6TN6 · X-ray structure of the endo-beta-1,4-mannanase from Thermotoga petrophila · the same entry in another collection · chain A against A, TM-score 1.00

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