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AlphaFold monomer V2.0 prediction for gamma- glutamylaminecyclotransferase (Q9BVM4)

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

Accession: Q9BVM4
Type: protein
Length: 153 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
UniProt: Q9BVM4

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	153	—	Q9BVM4

Compared structures

3JUC · Human gamma-glutamylamine cyclotransferase complex with 5-oxoproline · an experimental structure of the same protein · chain A against A, TM-score 0.95
3JUC · Human gamma-glutamylamine cyclotransferase complex with 5- oxoproline · an experimental structure of the same protein · chain A against A, TM-score 0.95
3JUD · Human gamma-glutamylamine cyclotransferase, E82Q mutant · an experimental structure of the same protein · chain A against A, TM-score 0.93
3JUD · Human gamma-glutamylamine cyclotransferase, E82Q mutant · an experimental structure of the same protein · chain A against A, TM-score 0.93
3JUB · Human gamma-glutamylamine cyclotransferase · an experimental structure of the same protein · chain A against A, TM-score 0.92
3JUB · Human gamma-glutamylamine cyclotransferase · an experimental structure of the same protein · chain A against A, 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 Q9BVM4
Elsewhere: UniProt Q9BVM4 · AlphaFold DB Q9BVM4

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