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Crystal structure of a putative alpha-GALACTOSIDASE/MELIBIASE (BF4189) from bacteroides fragilis nctc 9343 at 2.00 a resolution

Analyse Crystal structure of a putative alpha-GALACTOSIDASE/MELIBIASE (BF4189) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4OGZ
Type
protein
Length
927 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative alpha-GALACTOSIDASE/MELIBIASE
EC
3.2.1.22
UniProt
Q5L7T7
Ligands
PO4
Pockets
7 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative alpha-GALACTOSIDASE/MELIBIASE (EC 3.2.1.22)protein46123% helix, 28% strandQ5L7T7
BPutative alpha-GALACTOSIDASE/MELIBIASE (EC 3.2.1.22)protein46624% helix, 28% strandQ5L7T7

Ligands and binding sites

  • PO4 · Phosphate ion · ion · chains B
  • PEG · Di(hydroxyethyl)ether · additive · 8 copies · chains A, B
  • PGE · Triethylene glycol · additive · 2 copies · chains A

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12090.800.9438PEG
22170.780.9242PGE
39580.710.7569PEG
41290.390.7420PEG
51350.380.7325PEG

Interfaces

1 interface between chains.

  • A–B · 481 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified, 2 disulfide (engineered, disulfide).

Compared structures

  • 4OGZ · Crystal structure of a putative alpha-galactosidase/melibiase (BF4189) from Bacteroides… · the same entry in another collection · chain A against A, TM-score 1.00

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