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Ribonucleotide reductase Y122 2,3,5-F3Y variant

Analyse Ribonucleotide reductase Y122 2,3,5-F3Y variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5CI3
Type
protein
Length
349 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribonucleoside-diphosphate reductase 1 subunit beta
EC
1.17.4.1
UniProt
P69925
Ligands
FEO, SO4
Pockets
1 · best druggability 0.27

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibonucleoside-diphosphate reductase 1 subunit beta (EC 1.17.4.1)protein34969% helix, 4% strandP69925

Ligands and binding sites

  • FEO · Mu-oxo-diiron · ligand · chains A
  • SO4 · Sulfate ion · ion · 4 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1510.270.7414empty

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

  • 5CI3 · Ribonucleotide reductase Y122 2,3,5-F3Y variant · the same entry in another collection · chain A against A, TM-score 1.00
  • P69925 · AlphaFold monomer V2.0 prediction for ribonucleoside-diphosphate reductase 1 subunit beta… · a predicted model of the same protein · chain A against A, TM-score 1.00

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