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Helicase Sen1

Analyse Helicase Sen1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5MZN
Type
protein
Length
682 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.787
Source
Saccharomyces cerevisiae S288c
Molecule
Helicase SEN1,Helicase SEN1
EC
3.6.4.-
UniProt
Q00416
Ligands
ADP, MG
Pockets
9 · best druggability 0.54

Structure

x-ray diffraction · resolution 1.787 · 1 distinct chain · 42% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHelicase SEN1,Helicase SEN1 (EC 3.6.4.-)protein68242% helix, 19% strandQ00416

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • MG · Magnesium ion · metal · chains A
  • EDO · 1,2-ethanediol · additive · 40 copies · chains A
  • GOL · Glycerol · additive · 12 copies · chains A
  • PEG · Di(hydroxyethyl)ether · additive · 11 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13110.540.7535EDO
22740.520.7534ADP, EDO, PEG, MG
31940.490.7628EDO
4800.480.8219empty
51630.460.7626empty

Modifications

Observed in the structure: 2 covalent (additive adduct).

Compared structures

  • 5MZN · Helicase SEN1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q00416 · AlphaFold monomer V2.0 prediction for helicase SEN1 (Q00416) · a predicted model of the same protein · chain A against A, TM-score 0.97

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