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AlphaFold monomer V2.0 prediction for 3-hydroxyacyl-[acyl-carrier- protein] dehydratase fabz (A1VXZ7)

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

Accession: A1VXZ7
Type: protein
Length: 146 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
UniProt: A1VXZ7

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	146	—	A1VXZ7

Compared structures

3D6X · Crystal structure of campylobacter jejuni fabz · an experimental structure of the same protein · chain A against B, TM-score 0.94
3D6X · Crystal structure of Campylobacter jejuni FabZ · an experimental structure of the same protein · chain A against B, TM-score 0.94

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 A1VXZ7
Elsewhere: UniProt A1VXZ7 · AlphaFold DB A1VXZ7

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