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AlphaFold monomer V2.0 prediction for adenylyl cyclase-associated protein 1 (P40124)

Analyse AlphaFold monomer V2.0 prediction for adenylyl cyclase-associated protein 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P40124
Type: protein
Length: 474 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x8015C13fB5918822c590F95390BE1a831796bba2
UniProt: P40124

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	474	—	P40124

Compared structures

6RSQ · Helical folded domain of mouse CAP1 · an experimental structure of the same protein · chain A against C, TM-score 0.36
6RSQ · Helical folded domain of mouse CAP1 · an experimental structure of the same protein · chain A against C, TM-score 0.36
6RSW · HFD domain of mouse CAP1 bound to the pointed end of G-actin · an experimental structure of the same protein · chain A against C, TM-score 0.36
6RSW · Hfd domain of mouse CAP1 bound to the pointed end of G-actin · an experimental structure of the same protein · chain A against C, TM-score 0.36
6FM2 · CARP domain of mouse cyclase-associated protein 1 (CAP1) bound to ADP-actin · an experimental structure of the same protein · chain A against B, TM-score 0.33
6FM2 · Carp domain of mouse cyclase-associated protein 1 (CAP1) bound to ADP- actin · an experimental structure of the same protein · chain A against B, TM-score 0.33

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 P40124
Elsewhere: UniProt P40124 · AlphaFold DB P40124

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