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Crystal structure of hrpe and D-ribulose-5-phospate complex

Analyse Crystal structure of hrpe and D-ribulose-5-phospate complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OVQ
Type
protein
Length
438 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribulose-phosphate 3-epimerase
EC
5.1.3.1
UniProt
Q96AT9
Ligands
5RP, FE2
Pockets
4 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibulose-phosphate 3-epimerase (EC 5.1.3.1)protein21944% helix, 21% strandQ96AT9
BRibulose-phosphate 3-epimerase (EC 5.1.3.1)protein21941% helix, 21% strandQ96AT9

Ligands and binding sites

  • 5RP · Ribulose-5-phosphate · ligand · 2 copies · chains A, B
  • FE2 · Fe (II) ion · metal · 2 copies · chains A, B
  • XPE · 3,6,9,12,15,18,21,24,27-nonaoxanonacosane-1,29-diol · additive · 7 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1690.660.94265RP
21050.630.88325RP
3610.300.7513empty
4570.280.7513empty

Interfaces

1 interface between chains.

  • A–B · 1099 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 3OVQ · Crystal Structure of hRPE and D-Ribulose-5-Phospate Complex · the same entry in another collection · chain A against A, TM-score 1.00
  • Q96AT9 · AlphaFold monomer V2.0 prediction for ribulose-phosphate 3-epimerase (Q96AT9) · a predicted model of the same protein · chain A against A, TM-score 0.99

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