MolNFT v1 · #146771 · protein

AlphaFold monomer V2.0 prediction for ADP-ribosylation factor-binding protein GGA3 (Q9NZ52)

Q9NZ52: “AlphaFold monomer V2.0 prediction for ADP-ribosylation factor-binding protein GGA3 (Q9NZ52)”. MolNFT v1 #146771 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

Accession: Q9NZ52
Type: protein
Length: 723 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
UniProt: Q9NZ52

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	723	—	Q9NZ52

Compared structures

1JPL · GGA3 vhs domain complexed with C-terminal peptide from cation-independent mannose… · an experimental structure of the same protein · chain A against D, TM-score 0.21
1JPL · GGA3 VHS domain complexed with C-terminal peptide from cation-independent mannose… · an experimental structure of the same protein · chain A against D, TM-score 0.21
1JUQ · GGA3 vhs domain complexed with C-terminal peptide from cation- dependent mannose… · an experimental structure of the same protein · chain A against B, TM-score 0.21
1JUQ · GGA3 VHS domain complexed with C-terminal peptide from cation-dependent Mannose… · an experimental structure of the same protein · chain A against B, TM-score 0.21
1LF8 · Complex of GGA3-VHS Domain and CI-MPR C-terminal Phosphopeptide · an experimental structure of the same protein · chain A against B, TM-score 0.21
1LF8 · Complex of GGA3-vhs domain and ci-mpr C-terminal phosphopeptide · an experimental structure of the same protein · chain A against B, TM-score 0.21

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 Q9NZ52
Elsewhere: UniProt Q9NZ52 · AlphaFold DB Q9NZ52

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