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Type I-F anti-CRISPR protein ACRIF13

Analyse Type I-F anti-CRISPR protein ACRIF13 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7VEH
Type
protein
Length
934 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ACRIF13
UniProt
A0A3A9QXE8
Pockets
14 · best druggability 0.77

Structure

x-ray diffraction · 4 distinct chains · 25% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, D, F, GACRIF13protein11825% helix, 30% strandA0A3A9QXE8
B, CACRIF13protein11525% helix, 30% strandA0A3A9QXE8
EACRIF13protein11525% helix, 31% strandA0A3A9QXE8
HACRIF13protein11725% helix, 26% strandA0A3A9QXE8

Pockets

14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12850.770.8930empty
23760.760.8744empty
32780.760.8836empty
42450.710.8632empty
51850.570.8136empty

Interfaces

9 interfaces between chains.

  • A–D · 648 Ų buried · 13 hydrogen bonds · protein-protein
  • B–G · 640 Ų buried · 10 hydrogen bonds · protein-protein
  • B–C · 609 Ų buried · 11 hydrogen bonds · protein-protein
  • A–E · 608 Ų buried · 7 hydrogen bonds · protein-protein
  • C–D · 601 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 7VEH · Type I-F Anti-CRISPR protein AcrIF13 · the same entry in another collection · chain A against A, TM-score 1.00

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