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Characterization and structural analysis of a thermostable zearalenone-degrading enzyme

Analyse Characterization and structural analysis of a thermostable… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6L7M
Type
protein
Length
1,068 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ab hydrolase-1 domain-containing protein
UniProt
A0A4Q4UBE4
Pockets
6 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DAb hydrolase-1 domain-containing proteinprotein26747% helix, 17% strandA0A4Q4UBE4

Pockets

6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12320.800.9341empty
23190.800.9046empty
31620.790.9434empty
41020.730.9426empty
5600.720.9817empty

Interfaces

4 interfaces between chains.

  • B–D · 759 Ų buried · 14 hydrogen bonds · protein-protein
  • A–C · 742 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 717 Ų buried · 11 hydrogen bonds · protein-protein
  • C–D · 691 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 6L7M · Characterization and structural analysis of a thermostable zearale -degrading enzyme · the same entry in another collection · chain A against A, TM-score 1.00

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