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Crystal structure of the double mutant (CYS211SER/CYS292SER) 6- phospho-B-D-glucosidase from lactobacillus plantarum

Analyse Crystal structure of the double mutant (CYS211SER/CYS292SER) 6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5NAV
Type
protein
Length
2,766 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-galactosidase
EC
3.2.1.21
UniProt
F9ULH8
Pockets
20 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FBeta-galactosidase (EC 3.2.1.21)protein46145% helix, 17% strandF9ULH8

Pockets

20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16060.770.8349empty
26570.750.8050empty
35510.740.8239empty
45960.740.8144empty
55980.740.8136empty

Interfaces

6 interfaces between chains.

  • B–E · 734 Ų buried · 6 hydrogen bonds · protein-protein
  • A–F · 730 Ų buried · 6 hydrogen bonds · protein-protein
  • D–F · 362 Ų buried · 5 hydrogen bonds · protein-protein
  • D–E · 357 Ų buried · 0 hydrogen bonds · protein-protein
  • A–B · 142 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 5NAV · Crystal structure of the double mutant (Cys211Ser/Cys292Ser) 6-phospho-b-D-glucosidase… · the same entry in another collection · chain A against A, TM-score 1.00

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