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AlphaFold monomer V2.0 prediction for CRISPR-associated protein CASA/CSE1 (Q53VY1)

Analyse AlphaFold monomer V2.0 prediction for CRISPR-associated protein CASA/CSE1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q53VY1
Type: protein
Length: 502 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xa0b0c5caDD2aa61Cd32a103C8481800e4501Bfda
UniProt: Q53VY1

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	502	—	Q53VY1

Compared structures

4F3E · Crystal Structure of Thermus thermophilus HB8 CasA · an experimental structure of the same protein · chain A against A, TM-score 0.93
4F3E · Crystal structure of thermus thermophilus HB8 casa · an experimental structure of the same protein · chain A against A, TM-score 0.93
4AN8 · Structure of Thermus thermophilus CasA (Cse1) · an experimental structure of the same protein · chain A against A, TM-score 0.92
4AN8 · Structure of thermus thermophilus casa (CSE1) · an experimental structure of the same protein · chain A against A, TM-score 0.92
4EJ3 · Crystal structure of a CRISPR associated protein from Thermus thermophilus HB8 · an experimental structure of the same protein · chain A against B, TM-score 0.92
4EJ3 · Crystal structure of a CRISPR associated protein from thermus thermophilus HB8 · an experimental structure of the same protein · chain A against B, TM-score 0.92

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q53VY1
Elsewhere: UniProt Q53VY1 · AlphaFold DB Q53VY1

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