3RQS
Crystal Structure of human L-3- Hydroxyacyl-CoA dehydrogenase (EC1.1.1.35) from mitochondria at the resolution 2.0 A, Northeast Structural Genomics Consortium Target HR487, Mitochondrial Protein Partnership
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003857 | molecular_function | (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
| 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 | 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 | (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
| 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 | 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 | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 315 |
| Chain | Residue |
| A | ASN220 |
| A | VAL224 |
| A | VAL265 |
| A | THR269 |
| A | THR270 |
| A | ILE273 |
| A | GOL316 |
| A | HOH373 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 316 |
| Chain | Residue |
| A | TYR264 |
| A | GOL315 |
| A | GOL317 |
| A | HOH371 |
| B | GLY251 |
| A | ASN173 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 317 |
| Chain | Residue |
| A | MSE178 |
| A | PRO255 |
| A | MSE256 |
| A | LEU261 |
| A | GOL316 |
| A | HOH385 |
| B | ALA252 |
| B | HOH423 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 318 |
| Chain | Residue |
| A | PRO86 |
| A | LYS87 |
| A | GLU140 |
| A | ARG165 |
| A | LYS192 |
| A | HOH382 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 315 |
| Chain | Residue |
| B | ASN220 |
| B | VAL224 |
| B | VAL265 |
| B | THR269 |
| B | THR270 |
| B | ILE273 |
| B | GOL317 |
| B | HOH368 |
| B | HOH531 |
| B | HOH552 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 316 |
| Chain | Residue |
| B | MSE38 |
| B | ALA119 |
| B | ILE120 |
| B | GLU122 |
| B | ASN147 |
| B | HOH332 |
| B | HOH354 |
| B | HOH449 |
| B | HOH524 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 317 |
| Chain | Residue |
| A | GLY251 |
| A | HOH394 |
| B | PHE172 |
| B | ASN173 |
| B | LEU223 |
| B | VAL265 |
| B | GOL315 |
| B | HOH356 |
Functional Information from PROSITE/UniProt
| site_id | PS00067 |
| Number of Residues | 25 |
| Details | 3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. DtpGFIvNRllvPYLmeair.LYerG |
| Chain | Residue | Details |
| A | ASP213-GLY237 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10231530","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10840044","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10840044","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| 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 | 16 |
| 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 | 4 |
| 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 | 2 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 336 |
| Chain | Residue | Details |
| A | ARG165 | electrostatic stabiliser, hydrogen bond donor |
| A | THR186 | proton acceptor, proton donor |
| A | LYS202 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
| A | ILE244 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 336 |
| Chain | Residue | Details |
| B | ARG165 | electrostatic stabiliser, hydrogen bond donor |
| B | THR186 | proton acceptor, proton donor |
| B | LYS202 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
| B | ILE244 | electrostatic stabiliser, hydrogen bond donor |
