PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15690204-2 2005 Conserved glycines, Gly139 and Gly143, in the distal helix of human heme oxygenase-1 (HO-1) provide the flexibility required for the opening and closing of the heme active site for substrate binding and product dissociation during HO-1 catalysis. Glycine 10-18 heme oxygenase 1 Homo sapiens 68-84 15690204-2 2005 Conserved glycines, Gly139 and Gly143, in the distal helix of human heme oxygenase-1 (HO-1) provide the flexibility required for the opening and closing of the heme active site for substrate binding and product dissociation during HO-1 catalysis. Glycine 10-18 heme oxygenase 1 Homo sapiens 86-90 15690204-2 2005 Conserved glycines, Gly139 and Gly143, in the distal helix of human heme oxygenase-1 (HO-1) provide the flexibility required for the opening and closing of the heme active site for substrate binding and product dissociation during HO-1 catalysis. Glycine 10-18 heme oxygenase 1 Homo sapiens 231-235