8esi | pdb_00008esi

Bile Salt Hydrolase from B. longum with covalent inhibitor bound

spinqualitylabelsall models 8esi, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8esi is a 8 chain structure with sequence from Bifidobacterium longum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.35Å Ligands: WSR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CBH_BIFLN Bile salt hydrolase that catalyzes the deconjugation of glycine- and taurine-linked bile salts, which occurs naturally in the intestines of humans, releasing amino acid residues and deconjugated bile salts (bile acids). Can hydrolyze the amid bond in all six major human bile salts, namely glycocholate (GCA), glycodeoxycholate (GDCA), glycochenodeoxycholate (GCDCA), taurocholate (TCA), taurodeoxycholate (TDCA) and taurochenodeoxycholate (TCDCA). Shows a slight preference for glycine-conjugated bile acids as substrates (PubMed:10831430, PubMed:16905539). Is totally inactive toward penicillin V (PubMed:16905539).

Proteopedia Page Contributors and Editors (what is this?)

OCA