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CSF5, CRISPR-CAS type IV CAS6 crrna endonuclease

Analyse CSF5, CRISPR-CAS type IV CAS6 crrna endonuclease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6H9H
Type
protein + RNA
Length
547 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CSF5; Crrna
UniProt
Q5NWP0
Ligands
MN
Pockets
13 · best druggability 0.54

Structure

x-ray diffraction · 3 distinct chains · 30% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B, ACSF5protein25030% helix, 36% strandQ5NWP0
DCrrnarna23——
ECrrnarna24——

Ligands and binding sites

  • MN · Manganese (II) ion · metal · chains B, A
  • TLA · L(+)-tartaric acid · additive · 4 copies · chains A, D, B, E
  • GOL · Glycerol · additive · chains B, E

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1620.540.8820GOL
21660.490.7826TLA
31860.480.7629empty
41240.470.7917empty
51000.430.7821empty

Interfaces

3 interfaces between chains.

  • A–D · 2179 Ų buried · 67 hydrogen bonds · protein-nucleic
  • B–E · 2167 Ų buried · 67 hydrogen bonds · protein-nucleic
  • B–A · 410 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nucleotide modification).

Compared structures

  • 6H9H · Csf5, CRISPR-Cas type IV Cas6 crRNA endonuclease · the same entry in another collection · chain B against B, TM-score 1.00

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