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The structure of bacillus subtilis rbsd complexed with glycerol

Analyse The structure of bacillus subtilis rbsd complexed with glycerol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1OGF
Type
protein
Length
655 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
High affinity ribose transport protein rbsd
UniProt
P36946
Ligands
CL
Pockets
19 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, EHigh affinity ribose transport protein rbsdprotein13134% helix, 24% strandP36946

Ligands and binding sites

  • CL · Chloride ion · ion · 2 copies · chains A, D
  • GOL · Glycerol · additive · 5 copies · chains A, E, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11660.520.7827empty
21610.510.7823empty
31710.510.7829CL
41670.490.7730empty
51440.480.7824empty

Interfaces

5 interfaces between chains.

  • B–C · 440 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 435 Ų buried · 5 hydrogen bonds · protein-protein
  • D–E · 432 Ų buried · 4 hydrogen bonds · protein-protein
  • A–E · 428 Ų buried · 3 hydrogen bonds · protein-protein
  • C–D · 426 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 1OGF · The Structure of Bacillus subtilis RbsD complexed with glycerol · the same entry in another collection · chain B against B, TM-score 1.00
  • P36946 · AlphaFold monomer V2.0 prediction for D-ribose pyranase (P36946) · a predicted model of the same protein · chain A against A, TM-score 0.98

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