This is a family of proteins of 115 residues on average. The family has two highly conserved tryptophan residues. The fold is very similar to the lipocalin-like fold from several comparable structures.
","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Lipocalin","extract":"The lipocalins are a family of proteins which transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids, and most lipocalins are also able to bind to complexed iron as well as heme. They share limited regions of sequence homology and a common tertiary structure architecture. This is an eight stranded antiparallel beta barrel with a repeated + 1 topology enclosing an internal ligand binding site.
","thumbnail":null}],"literature":null,"set_info":{"accession":"CL0116","name":"Calycin"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":9,"interactions":0,"matches":259,"pathways":0,"proteins":259,"proteomes":229,"sets":1,"structural_models":{"alphafold":184},"structures":1,"taxa":432},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":11,"alignment:full":151},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"3hty","name":"Crystal structure of a lipocalin-like protein (BT_0869) from Bacteroides thetaiotaomicron VPI-5482 at 1.95 A resolution"}}}