3HDH
PIG HEART SHORT CHAIN L-3-HYDROXYACYL COA DEHYDROGENASE REVISITED: SEQUENCE ANALYSIS AND CRYSTAL STRUCTURE DETERMINATION
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
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 | 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 | 0030154 | biological_process | cell differentiation |
A | 0042802 | molecular_function | identical protein binding |
A | 0050796 | biological_process | regulation of insulin secretion |
A | 0070403 | molecular_function | NAD+ binding |
B | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
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 | 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 | 0030154 | biological_process | cell differentiation |
B | 0042802 | molecular_function | identical protein binding |
B | 0050796 | biological_process | regulation of insulin secretion |
B | 0070403 | molecular_function | NAD+ binding |
C | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
C | 0005739 | cellular_component | mitochondrion |
C | 0005759 | cellular_component | mitochondrial matrix |
C | 0006631 | biological_process | fatty acid metabolic process |
C | 0006635 | biological_process | fatty acid beta-oxidation |
C | 0007283 | biological_process | spermatogenesis |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0030154 | biological_process | cell differentiation |
C | 0042802 | molecular_function | identical protein binding |
C | 0050796 | biological_process | regulation of insulin secretion |
C | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NAD A 350 |
Chain | Residue |
A | LEU25 |
A | LYS115 |
A | ASN135 |
A | SER137 |
A | HIS158 |
A | PHE159 |
A | MET26 |
A | ASP45 |
A | GLN46 |
A | ALA107 |
A | ILE108 |
A | VAL109 |
A | GLU110 |
A | VAL114 |
site_id | AC2 |
Number of Residues | 12 |
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 | PHE159 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NAD C 1150 |
Chain | Residue |
C | GLY22 |
C | LEU25 |
C | MET26 |
C | ASP45 |
C | GLN46 |
C | ALA107 |
C | ILE108 |
C | GLU110 |
C | LYS115 |
C | LEU118 |
C | ASN135 |
C | THR136 |
C | SER137 |
C | HIS158 |
C | PHE159 |
C | ASN161 |
Functional Information from PROSITE/UniProt
site_id | PS00067 |
Number of Residues | 25 |
Details | 3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. DtpGFIvNRllvPYLieavr.LYerG |
Chain | Residue | Details |
A | ASP201-GLY225 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 15 |
Details | BINDING: BINDING => ECO:0000269|PubMed:3479790 |
Chain | Residue | Details |
A | ALA34 | |
B | THR149 | |
C | ALA34 | |
C | GLY57 | |
C | LEU122 | |
C | ALA127 | |
C | THR149 | |
A | GLY57 | |
A | LEU122 | |
A | ALA127 | |
A | THR149 | |
B | ALA34 | |
B | GLY57 | |
B | LEU122 | |
B | ALA127 |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q16836 |
Chain | Residue | Details |
A | ASN73 | |
A | PHE80 | |
A | LYS173 | |
B | ASN73 | |
B | PHE80 | |
B | LYS173 | |
C | ASN73 | |
C | PHE80 | |
C | LYS173 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | SITE: Important for catalytic activity => ECO:0000250|UniProtKB:Q16836 |
Chain | Residue | Details |
A | GLU170 | |
B | GLU170 | |
C | GLU170 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q61425 |
Chain | Residue | Details |
A | PHE80 | |
A | ILE206 | |
B | PHE80 | |
B | ILE206 | |
C | PHE80 | |
C | ILE206 |
site_id | SWS_FT_FI5 |
Number of Residues | 24 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425 |
Chain | Residue | Details |
A | VAL81 | |
B | SER87 | |
B | THR136 | |
B | LEU185 | |
B | LEU192 | |
B | THR202 | |
B | VAL212 | |
B | GLY241 | |
C | VAL81 | |
C | SER87 | |
C | THR136 | |
A | SER87 | |
C | LEU185 | |
C | LEU192 | |
C | THR202 | |
C | VAL212 | |
C | GLY241 | |
A | THR136 | |
A | LEU185 | |
A | LEU192 | |
A | THR202 | |
A | VAL212 | |
A | GLY241 | |
B | VAL81 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q61425 |
Chain | Residue | Details |
A | PHE125 | |
A | GLN179 | |
B | PHE125 | |
B | GLN179 | |
C | PHE125 | |
C | GLN179 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:Q16836 |
Chain | Residue | Details |
A | ALA127 | |
B | ALA127 | |
C | ALA127 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 2hdh |
Chain | Residue | Details |
A | ASN208 | |
A | SER137 | |
A | HIS158 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 2hdh |
Chain | Residue | Details |
B | ASN208 | |
B | SER137 | |
B | HIS158 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 2hdh |
Chain | Residue | Details |
C | ASN208 | |
C | SER137 | |
C | HIS158 |