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Crystal structure of CRISPR-associated protein

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

PDB
3VZI
Type
protein
Length
427 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CRISPR-associated protein CAS5, dvulg subtype
UniProt
B2SNP4
Pockets
5 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACRISPR-associated protein CAS5, dvulg subtypeprotein21421% helix, 35% strandB2SNP4
BCRISPR-associated protein CAS5, dvulg subtypeprotein21321% helix, 35% strandB2SNP4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11270.610.8528empty
21240.530.8226empty
3910.470.8129empty
41470.400.7430empty
51000.360.7423empty

Interfaces

1 interface between chains.

  • A–B · 658 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 3VZI · Crystal Structure of CRISPR-associated Protein · the same entry in another collection · chain A against A, TM-score 1.00

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