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Crystal structure of CSM6 in complex with A4>P by soaking A4>P into CSM6

Analyse Crystal structure of CSM6 in complex with A4>P by soaking A4>P into CSM6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6OV0
Type
protein + RNA
Length
1,742 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uncharacterized protein; RNA (5'-R(*AP*AP*AP*(A23))-3')
UniProt
B6YWC3
Pockets
20 · best druggability 0.86

Structure

x-ray diffraction · 4 distinct chains · 47% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CUncharacterized proteinprotein43347% helix, 21% strandB6YWC3
B, DUncharacterized proteinprotein43247% helix, 20% strandB6YWC3
E, HRNA (5'-R(*AP*AP*AP*(A23))-3')rna4——
F, GRNA (5'-R(*AP*AP*AP*(A23))-3')rna2——

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111710.860.8779empty
211780.860.8780empty
35240.630.7649empty
42780.540.7625empty
52550.530.7619empty

Interfaces

11 interfaces between chains.

  • C–D · 2358 Ų buried · 19 hydrogen bonds · protein-protein
  • A–B · 2354 Ų buried · 18 hydrogen bonds · protein-protein
  • B–D · 523 Ų buried · 3 hydrogen bonds · protein-protein
  • D–H · 511 Ų buried · 12 hydrogen bonds · protein-nucleic
  • A–E · 501 Ų buried · 13 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 4 modified (nucleotide modification).

Compared structures

  • 6OV0 · Crystal structure of Csm6 in complex with A4>p by soaking A4>p into Csm6 · the same entry in another collection · chain A against A, TM-score 1.00

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