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MolNFT v1 · #17032 · protein

The structure of bacillus subtilis rbsd complexed with ribose 5- phosphate

1OGE · High affinity ribose transport protein rbsd: “The structure of bacillus subtilis rbsd complexed with ribose 5- phosphate”. X-ray diffraction, 2 ligands (RP5, CL), 20 pockets (best druggability 0.52). MolNFT v1 #17032 on GenesisL1…

PDB
1OGE
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
RP5, CL
Pockets
20 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, EHigh affinity ribose transport protein rbsdprotein13134% helix, 23% strandP36946

Ligands and binding sites

  • RP5 · 5-O-phosphono-beta-D-ribofuranose · ligand · 5 copies · chains A, E, B, C, D
  • CL · Chloride ion · ion · 2 copies · chains A, D

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

Pockets

20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11620.520.7920empty
21840.520.7825empty
31730.510.7726empty
41870.500.7728empty
51580.490.7724empty

Interfaces

5 interfaces between chains.

  • A–B · 411 Ų buried · 4 hydrogen bonds · protein-protein
  • B–C · 408 Ų buried · 3 hydrogen bonds · protein-protein
  • D–E · 405 Ų buried · 3 hydrogen bonds · protein-protein
  • C–D · 403 Ų buried · 3 hydrogen bonds · protein-protein
  • A–E · 401 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 1OGE · The Structure of Bacillus subtilis RbsD complexed with Ribose 5-phosphate · the same entry in another collection · chain A against A, 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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