PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 14735332-8 2004 Significantly,5 maintains the key features observed in the active site of ACS, namely a square-planar Ni coordinated to two deprotonated amides and two thiolates, where the thiolates bridge to a second metal, suggesting that 5 is a reasonable structural model for this unique enzyme. Amides 137-143 acyl-CoA synthetase short chain family member 2 Homo sapiens 74-77 14735332-0 2004 Modeling carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS): a trinuclear nickel complex employing deprotonated amides and bridging thiolates. Amides 122-128 acyl-CoA synthetase short chain family member 2 Homo sapiens 60-69 14735332-1 2004 Carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) utilizes a unique Ni-M bimetallic site in the biosynthesis of acetyl-CoA, where a square-planar Ni ion is coordinated to two thiolates and two deprotonated amides in a Cys-Gly-Cys motif. Amides 217-223 acyl-CoA synthetase short chain family member 2 Homo sapiens 51-59 34917239-0 2021 Amide-Substituted Condensed Pyridine Derivatives as ACSS2 Inhibitors for Treating Cancer. Amides 0-5 acyl-CoA synthetase short chain family member 2 Homo sapiens 52-57 21666847-1 2011 Nickel Superoxide Dismutase (NiSOD) and the A-cluster of Carbon Monoxide Dehydrogenase/Acetyl Coenzyme A Synthase (CODH/ACS) both feature active sites with Ni coordinated by thiolate and amide donors. Amides 187-192 acyl-CoA synthetase short chain family member 2 Homo sapiens 115-123