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Structure of an antibiotic related methyltransferase

Analyse Structure of an antibiotic related methyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3P2I
Type
protein
Length
398 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
16S rRNA methylase
UniProt
A8C927
Pockets
7 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B16S rRNA methylaseprotein19937% helix, 30% strandA8C927

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16300.770.8274empty
2980.730.9519empty
32690.540.7634empty
4650.360.7817empty
5690.360.7715empty

Interfaces

1 interface between chains.

  • A–B · 977 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 3P2I · Structure of an antibiotic related Methyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
  • A8C927 · AlphaFold monomer V2.0 prediction for 16S rRNA (ADENINE(1408)-N(1))-methyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

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