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Structure of escherichia COLI ribose-5-phosphate isomerase, rpia, complexed with arabinose-5-phosphate.

Analyse Structure of escherichia COLI ribose-5-phosphate isomerase, rpia, complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1O8B
Type
protein
Length
380 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribose 5-phosphate isomerase
EC
5.3.1.6
UniProt
P0A7Z0
Ligands
ABF
Pockets
5 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibose 5-phosphate isomerase (EC 5.3.1.6)protein16823% helix, 36% strandP0A7Z0
BRibose 5-phosphate isomerase (EC 5.3.1.6)protein21234% helix, 30% strandP0A7Z0

Ligands and binding sites

  • ABF · 5-O-phosphono-beta-D-arabinofuranose · ligand · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11160.460.7821empty
21230.420.7620empty
3680.360.7820ABF
4520.330.7817ABF
5540.310.7616empty

Interfaces

1 interface between chains.

  • A–B · 1110 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 11 modified (engineered).

Compared structures

  • 1O8B · Structure of Escherichia coli ribose-5-phosphate isomerase, RpiA, complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A7Z0 · AlphaFold monomer V2.0 prediction for ribose-5-phosphate isomerase a (P0A7Z0) · a predicted model of the same protein · chain B against A, TM-score 0.99

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