GL1X · GenesisL1 explorer

MolNFT v1 · #126621 · protein

Crystal structure of alpha-L-arabinofuranosidase from lactobacillus brevis

5M8B · Alpha-L-arabinofuranosidase II: “Crystal structure of alpha-L-arabinofuranosidase from lactobacillus brevis”. X-ray diffraction, 1 ligand (MG), 8 pockets (best druggability 0.71). MolNFT v1 #126621 on GenesisL1: 3D structure…

PDB
5M8B
Type
protein
Length
650 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-L-arabinofuranosidase II
EC
3.2.1.55
UniProt
A0A0D0G8J8
Ligands
MG
Pockets
8 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAlpha-L-arabinofuranosidase II (EC 3.2.1.55)protein3257% helix, 46% strandA0A0D0G8J8

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A, B
  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 4 copies · chains A, B
  • PGE · Triethylene glycol · additive · 2 copies · chains A
  • 1PE · Pentaethylene glycol · additive · chains A, B
  • PG4 · Tetraethylene glycol · additive · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15180.710.8064empty
23540.680.8135TRS, PGE
31240.680.9026TRS, PG4
43220.610.7829empty
52820.570.7727TRS

Interfaces

1 interface between chains.

  • A–B · 1424 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

  • 5M8B · Crystal structure of alpha-L-arabinofuranosidase from Lactobacillus brevis · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.