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Crystal structure of type I-D CRISPR-CAS nuclease CAS10D in complex with the SIRV3 ACRID1 (GP02) anti-CRISPR protein

Analyse Crystal structure of type I-D CRISPR-CAS nuclease CAS10D in complex with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6THH
Type
protein
Length
1,008 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SIRV3 ACRID1 (GP02) anti-CRISPR protein; CRISPR-associated protein, csca
UniProt
A0A1B3SN05, M9U4Y8
Ligands
ZN, PO4
Pockets
11 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BSIRV3 ACRID1 (GP02) anti-CRISPR proteinprotein9620% helix, 59% strandA0A1B3SN05
CCRISPR-associated protein, cscaprotein81655% helix, 6% strandM9U4Y8

Ligands and binding sites

  • ZN · Zinc ion · metal · chains C
  • PO4 · Phosphate ion · ion · chains C

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

Pockets

11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111430.820.83116empty
22370.720.8744empty
34100.700.8156empty
43290.610.7825empty
5780.500.8419empty

Interfaces

3 interfaces between chains.

  • A–B · 1009 Ų buried · 16 hydrogen bonds · protein-protein
  • A–C · 692 Ų buried · 10 hydrogen bonds · protein-protein
  • B–C · 322 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified, 2 disulfide (engineered, disulfide).

Compared structures

  • 6THH · Crystal structure of type I-D CRISPR-Cas nuclease Cas10d in complex with the SIRV3 AcrID1… · the same entry in another collection · chain A against A, TM-score 1.00

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