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Cryoem structure of ACRIIA2 homolog in complex with CRISPR-CAS9

Analyse Cryoem structure of ACRIIA2 homolog in complex with CRISPR-CAS9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6MCC
Type
protein + RNA
Length
1,610 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Single guide RNA (116-mer); CRISPR-associated endonuclease CAS9; Anti-CRISPR ACRIIA2…
EC
3.1.-.-
UniProt
J7M7J1
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 3 distinct chains · 38% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BSingle guide RNA (116-mer)rna116——
ACRISPR-associated endonuclease CAS9 (EC 3.1.-.-)protein136440% helix, 11% strandJ7M7J1
CAnti-CRISPR ACRIIA2 homologprotein13023% helix, 22% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110730.860.88105empty
26060.790.8556empty
33630.790.8944empty
45960.750.8264empty
51890.740.9138empty

Interfaces

3 interfaces between chains.

  • B–A · 7242 Ų buried · 139 hydrogen bonds · protein-nucleic
  • A–C · 1438 Ų buried · 9 hydrogen bonds · protein-protein
  • B–C · 126 Ų buried · 1 hydrogen bond · protein-nucleic

Modifications

Observed in the structure: 1 modified (nucleotide modification).

Compared structures

  • 6MCC · CryoEM structure of AcrIIA2 homolog in complex with CRISPR-Cas9 · the same entry in another collection · chain C against C, TM-score 1.00

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