1M75
Crystal Structure of the N208S Mutant of L-3-Hydroxyacyl-COA Dehydrogenase in Complex with NAD and Acetoacetyl-COA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006635 | biological_process | fatty acid beta-oxidation |
A | 0007283 | biological_process | spermatogenesis |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0009725 | biological_process | response to hormone |
A | 0014823 | biological_process | response to activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0016740 | molecular_function | transferase activity |
A | 0030154 | biological_process | cell differentiation |
A | 0032868 | biological_process | response to insulin |
A | 0042802 | molecular_function | identical protein binding |
A | 0046676 | biological_process | negative regulation of insulin secretion |
A | 0050796 | biological_process | regulation of insulin secretion |
A | 0070403 | molecular_function | NAD+ binding |
A | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
B | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006635 | biological_process | fatty acid beta-oxidation |
B | 0007283 | biological_process | spermatogenesis |
B | 0009410 | biological_process | response to xenobiotic stimulus |
B | 0009725 | biological_process | response to hormone |
B | 0014823 | biological_process | response to activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0016740 | molecular_function | transferase activity |
B | 0030154 | biological_process | cell differentiation |
B | 0032868 | biological_process | response to insulin |
B | 0042802 | molecular_function | identical protein binding |
B | 0046676 | biological_process | negative regulation of insulin secretion |
B | 0050796 | biological_process | regulation of insulin secretion |
B | 0070403 | molecular_function | NAD+ binding |
B | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE CAA A 351 |
Chain | Residue |
A | SER61 |
A | VAL165 |
A | MET166 |
A | SER208 |
A | LEU211 |
A | PRO243 |
A | MET244 |
A | LEU249 |
A | NAD350 |
A | HOH874 |
A | HOH944 |
A | VAL65 |
A | HOH960 |
B | GLY239 |
B | ALA240 |
B | HOH802 |
A | LYS68 |
A | SER137 |
A | HIS158 |
A | PHE160 |
A | ASN161 |
A | PRO162 |
A | PRO164 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE CAA B 751 |
Chain | Residue |
A | GLY239 |
A | ALA240 |
A | HOH819 |
B | SER61 |
B | VAL65 |
B | LYS68 |
B | SER137 |
B | PHE160 |
B | ASN161 |
B | PRO162 |
B | VAL165 |
B | MET166 |
B | SER208 |
B | LEU211 |
B | VAL212 |
B | PRO243 |
B | MET244 |
B | LEU249 |
B | TYR252 |
B | ILE261 |
B | NAD750 |
B | HOH1005 |
site_id | AC3 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NAD A 350 |
Chain | Residue |
A | ILE21 |
A | GLY24 |
A | LEU25 |
A | MET26 |
A | ASP45 |
A | ALA107 |
A | ILE108 |
A | GLU110 |
A | LYS115 |
A | ASN135 |
A | SER137 |
A | HIS158 |
A | PHE159 |
A | ASN161 |
A | VAL253 |
A | THR257 |
A | LYS293 |
A | CAA351 |
A | HOH801 |
A | HOH957 |
site_id | AC4 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAD B 750 |
Chain | Residue |
B | GLY24 |
B | LEU25 |
B | MET26 |
B | ASP45 |
B | GLN46 |
B | ALA107 |
B | ILE108 |
B | GLU110 |
B | LYS115 |
B | ASN135 |
B | SER137 |
B | HIS158 |
B | PHE159 |
B | ASN161 |
B | VAL253 |
B | LYS293 |
B | CAA751 |
B | HOH822 |
B | HOH823 |
B | HOH940 |
B | HOH949 |
B | HOH973 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044 |
Chain | Residue | Details |
A | GLY22 | |
B | GLU110 | |
B | LYS115 | |
B | SER137 | |
B | ASN161 | |
B | LYS293 | |
A | ASP45 | |
A | GLU110 | |
A | LYS115 | |
A | SER137 | |
A | ASN161 | |
A | LYS293 | |
B | GLY22 | |
B | ASP45 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10840044 |
Chain | Residue | Details |
A | SER61 | |
A | LYS68 | |
B | SER61 | |
B | LYS68 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Important for catalytic activity => ECO:0000305 |
Chain | Residue | Details |
A | HIS158 | |
B | HIS158 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 |
Chain | Residue | Details |
A | LYS68 | |
A | LYS194 | |
B | LYS68 | |
B | LYS194 |
site_id | SWS_FT_FI5 |
Number of Residues | 18 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 |
Chain | Residue | Details |
A | LYS69 | |
B | LYS69 | |
B | LYS75 | |
B | LYS124 | |
B | LYS173 | |
B | LYS180 | |
B | LYS190 | |
B | LYS200 | |
B | LYS229 | |
B | LYS300 | |
A | LYS75 | |
A | LYS124 | |
A | LYS173 | |
A | LYS180 | |
A | LYS190 | |
A | LYS200 | |
A | LYS229 | |
A | LYS300 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 |
Chain | Residue | Details |
A | LYS113 | |
A | LYS167 | |
B | LYS113 | |
B | LYS167 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674 |
Chain | Residue | Details |
A | LYS115 | |
B | LYS115 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 336 |
Chain | Residue | Details |
A | SER137 | electrostatic stabiliser, hydrogen bond donor |
A | HIS158 | proton acceptor, proton donor |
A | GLU170 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
A | SER208 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 336 |
Chain | Residue | Details |
B | SER137 | electrostatic stabiliser, hydrogen bond donor |
B | HIS158 | proton acceptor, proton donor |
B | GLU170 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
B | SER208 | electrostatic stabiliser, hydrogen bond donor |