3B96
Structural Basis for Substrate Fatty-Acyl Chain Specificity: Crystal Structure of Human Very-Long-Chain Acyl-CoA Dehydrogenase
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 | 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 | 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 | 10 |
| Details | BINDING SITE FOR RESIDUE MYA A 1 |
| Chain | Residue |
| A | TYR120 |
| A | HOH1002 |
| A | VAL124 |
| A | GLY135 |
| A | ILE144 |
| A | LEU297 |
| A | PHE421 |
| A | GLU422 |
| A | GLY423 |
| A | FAD616 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD A 616 |
| Chain | Residue |
| A | MYA1 |
| A | PHE174 |
| A | LEU176 |
| A | THR177 |
| A | GLY182 |
| A | SER183 |
| A | TRP209 |
| A | ILE210 |
| A | SER211 |
| A | ARG326 |
| A | GLN328 |
| A | PHE329 |
| A | ILE333 |
| A | PHE336 |
| A | GLN395 |
| A | ILE396 |
| A | GLY399 |
| A | ILE417 |
| A | PHE421 |
| A | THR424 |
| A | ASP426 |
| A | ILE427 |
| A | GLN522 |
| A | HOH639 |
| A | HOH654 |
| A | HOH668 |
| A | HOH680 |
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 | GLU422 |
| 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 | PHE174 | |
| A | TRP209 | |
| A | PHE421 | |
| A | THR424 | |
| A | GLN522 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P50544 |
| Chain | Residue | Details |
| A | LYS31 | |
| A | LYS199 | |
| A | LYS236 | |
| A | LYS238 | |
| A | LYS291 | |
| A | LYS442 | |
| A | LYS516 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P50544 |
| Chain | Residue | Details |
| A | LYS155 | |
| A | LYS332 | |
| A | LYS599 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P50544 |
| Chain | Residue | Details |
| A | CYS197 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P50544 |
| Chain | Residue | Details |
| A | LYS258 | |
| A | LYS510 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER477 | |
| A | SER482 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLY300 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLU422 |
