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Crystal structure of Escherichia coli ribosomal oxygenase YcfD

Analyse Crystal structure of Escherichia coli ribosomal oxygenase YcfD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4NUB
Type
protein
Length
361 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.7
Source
Escherichia coli
Molecule
50S ribosomal protein L16 arginine hydroxylase
EC
1.14.11.-
UniProt
P27431
Ligands
FE
Pockets
2 · best druggability 0.70

Structure

x-ray diffraction · resolution 2.7 · 1 distinct chain · 29% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A50S ribosomal protein L16 arginine hydroxylase (EC 1.14.11.-)protein36129% helix, 24% strandP27431

Ligands and binding sites

  • FE · Fe (III) ion · metal · chains A
  • GOL · Glycerol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12600.700.8630empty
23050.650.8140FE

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

  • 4NUB · Crystal structure of escherichia COLI ribosomal oxygenase ycfd · the same entry in another collection · chain A against A, TM-score 1.00
  • P27431 · AlphaFold monomer V2.0 prediction for 50S ribosomal protein L16 3-hydroxylase (P27431) · a predicted model of the same protein · chain A against A, TM-score 1.00

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