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Unlocking the structural features for the exo-xylobiosidase activity of an unusual GH11 member identified in a compost-derived consortium

Analyse Unlocking the structural features for the exo-xylobiosidase activity of an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7L1W
Type
protein
Length
245 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Exo-B-1,4-beta-xylanase
Pockets
1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AExo-B-1,4-beta-xylanaseprotein24511% helix, 48% strand—

Ligands and binding sites

  • MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

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
12530.580.7933empty

Compared structures

  • 7L1W · Unlocking the structural features for the exo-xylobiosidase activity of an unusual GH11… · the same entry in another collection · chain A against A, TM-score 1.00

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