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Crystal structure of anti-CRISPR protein ACRF10

Analyse Crystal structure of anti-CRISPR protein ACRF10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ANW
Type
protein
Length
282 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Anti-CRISPR protein ACRF10
UniProt
A0A073KP86
Pockets
2 · best druggability 0.44

Structure

x-ray diffraction · 3 distinct chains · 26% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAnti-CRISPR protein ACRF10protein9626% helix, 38% strandA0A073KP86
BAnti-CRISPR protein ACRF10protein9428% helix, 37% strandA0A073KP86
CAnti-CRISPR protein ACRF10protein9225% helix, 38% strandA0A073KP86

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11380.440.7626empty
2630.290.7414empty

Interfaces

2 interfaces between chains.

  • A–B · 303 Ų buried · 10 hydrogen bonds · protein-protein
  • A–C · 257 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 6ANW · Crystal structure of anti-CRISPR protein AcrF10 · the same entry in another collection · chain A against A, TM-score 1.00

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