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Crystal structure of L-arabinose isomerase from lactobacillus fermentum CGMCC2921

Analyse Crystal structure of L-arabinose isomerase from lactobacillus fermentum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4LQL
Type
protein
Length
2,844 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-arabinose isomerase
EC
5.3.1.4
UniProt
D9ILD9
Pockets
20 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FL-arabinose isomerase (EC 5.3.1.4)protein47427% helix, 14% strandD9ILD9

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17710.880.91129empty
23050.830.9454empty
33000.820.9255empty
44880.820.8888empty
53040.810.9252empty

Interfaces

12 interfaces between chains.

  • E–F · 1571 Ų buried · 9 hydrogen bonds · protein-protein
  • D–E · 1551 Ų buried · 24 hydrogen bonds · protein-protein
  • B–C · 1534 Ų buried · 15 hydrogen bonds · protein-protein
  • A–B · 1496 Ų buried · 10 hydrogen bonds · protein-protein
  • A–C · 1397 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 4LQL · Crystal structure of L-arabinose isomerase from Lactobacillus fermentum CGMCC2921 · the same entry in another collection · chain A against A, TM-score 1.00

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