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Reverse transcriptase domain of group II intron maturase from roseburia intestinalis in P1 space group

Analyse Reverse transcriptase domain of group II intron maturase from roseburia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5IRF
Type
protein
Length
1,142 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Retron-type reverse transcriptase
UniProt
D4L313
Ligands
K
Pockets
13 · best druggability 0.73

Structure

x-ray diffraction · 4 distinct chains · 49% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARetron-type reverse transcriptaseprotein28348% helix, 15% strandD4L313
BRetron-type reverse transcriptaseprotein28748% helix, 16% strandD4L313
CRetron-type reverse transcriptaseprotein28251% helix, 15% strandD4L313
DRetron-type reverse transcriptaseprotein29050% helix, 17% strandD4L313

Ligands and binding sites

  • K · Potassium ion · metal · 4 copies · chains A, B, C, D

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

Pockets

13 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18740.730.7884empty
25760.730.8148empty
36010.730.8061empty
45920.720.8049empty
55440.710.8051empty

Interfaces

5 interfaces between chains.

  • B–D · 1708 Ų buried · 36 hydrogen bonds · protein-protein
  • A–C · 1613 Ų buried · 36 hydrogen bonds · protein-protein
  • C–D · 357 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 304 Ų buried · 3 hydrogen bonds · protein-protein
  • B–C · 136 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5IRF · Reverse transcriptase domain of group II intron maturase from Roseburia intestinalis in… · the same entry in another collection · chain A against A, TM-score 1.00

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