2UXW
Crystal structure of human very long chain acyl-CoA dehydrogenase (ACADVL)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000062 | molecular_function | fatty-acyl-CoA binding |
| A | 0001659 | biological_process | temperature homeostasis |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0004466 | molecular_function | long-chain fatty acyl-CoA dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0009062 | biological_process | fatty acid catabolic process |
| A | 0009409 | biological_process | response to cold |
| A | 0015980 | biological_process | energy derivation by oxidation of organic compounds |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0017099 | molecular_function | very-long-chain fatty acyl-CoA dehydrogenase activity |
| A | 0030855 | biological_process | epithelial cell differentiation |
| A | 0031966 | cellular_component | mitochondrial membrane |
| A | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| A | 0042645 | cellular_component | mitochondrial nucleoid |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045717 | biological_process | negative regulation of fatty acid biosynthetic process |
| A | 0046322 | biological_process | negative regulation of fatty acid oxidation |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0090181 | biological_process | regulation of cholesterol metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 680 |
| Chain | Residue |
| A | PHE376 |
| A | PRO494 |
| A | PHE495 |
| A | GLN562 |
| A | FAD700 |
| A | HOH2405 |
| A | HOH2407 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 681 |
| Chain | Residue |
| A | ASP257 |
| A | ARG286 |
| A | GLY254 |
| A | LEU255 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD A 700 |
| Chain | Residue |
| A | PHE214 |
| A | LEU216 |
| A | THR217 |
| A | GLY222 |
| A | SER223 |
| A | TRP249 |
| A | ILE250 |
| A | SER251 |
| A | ARG366 |
| A | GLN368 |
| A | PHE369 |
| A | ILE373 |
| A | PHE376 |
| A | GLN435 |
| A | ILE436 |
| A | GLY439 |
| A | MET443 |
| A | ILE457 |
| A | PHE461 |
| A | THR464 |
| A | ASP466 |
| A | ILE467 |
| A | GLN562 |
| A | EDO680 |
| A | TH3750 |
| A | HOH2297 |
| A | HOH2352 |
| A | HOH2502 |
| A | HOH2503 |
| A | HOH2504 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TH3 A 750 |
| Chain | Residue |
| A | TYR160 |
| A | GLY175 |
| A | ILE184 |
| A | PHE214 |
| A | GLY222 |
| A | LEU337 |
| A | PHE461 |
| A | GLU462 |
| A | GLY463 |
| A | FAD700 |
| A | HOH2171 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:18227065, ECO:0000269|PubMed:9461620, ECO:0007744|PDB:2UXW, ECO:0007744|PDB:3B96 |
| Chain | Residue | Details |
| A | GLU462 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18227065, ECO:0007744|PDB:2UXW, ECO:0007744|PDB:3B96 |
| Chain | Residue | Details |
| A | PHE214 | |
| A | TRP249 | |
| A | PHE461 | |
| A | THR464 | |
| A | GLN562 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P50544 |
| Chain | Residue | Details |
| A | MET0 | |
| A | LYS239 | |
| A | LYS276 | |
| A | LYS278 | |
| A | LYS331 | |
| A | LYS482 | |
| A | LYS556 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P50544 |
| Chain | Residue | Details |
| A | LYS195 | |
| A | LYS372 | |
| A | LYS639 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P50544 |
| Chain | Residue | Details |
| A | CYS237 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P50544 |
| Chain | Residue | Details |
| A | LYS298 | |
| A | LYS550 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER517 | |
| A | SER522 |
