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Crystal structure of the alpha-L-arabinofuranosidase UMABF62A from ustilago maidys

Analyse Crystal structure of the alpha-L-arabinofuranosidase UMABF62A from ustilago… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4N1I
Type
protein
Length
312 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-L-arabinofuranosidase UMABF62A
EC
3.2.1.55
UniProt
Q4P6F4
Ligands
CA
Pockets
2 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-L-arabinofuranosidase UMABF62A (EC 3.2.1.55)protein3126% helix, 45% strandQ4P6F4

Ligands and binding sites

  • CA · Calcium ion · metal · chains A
  • GOL · Glycerol · additive · 4 copies · chains A
  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
  • 1PE · Pentaethylene glycol · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11320.440.7717empty
2720.410.8020GOL

Modifications

Observed in the structure: 1 covalent, 1 disulfide (additive adduct, disulfide).

Compared structures

  • 4N1I · Crystal Structure of the alpha-L-arabinofuranosidase UmAbf62A from Ustilago maidys · the same entry in another collection · chain A against A, TM-score 1.00

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