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 | (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0006629 | biological_process | lipid metabolic process |
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 |
A | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
B | 0003857 | molecular_function | (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0006629 | biological_process | lipid metabolic process |
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 |
B | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
C | 0003857 | molecular_function | (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
C | 0005654 | cellular_component | nucleoplasm |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005759 | cellular_component | mitochondrial matrix |
C | 0006629 | biological_process | lipid metabolic process |
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 |
C | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
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 | 27 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"3479790","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q16836","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"Q16836","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q61425","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 26 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q61425","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q61425","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"Q16836","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
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 |