2JIF
Structure of human short-branched chain acyl-CoA dehydrogenase (ACADSB)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A1436 |
| Chain | Residue |
| A | ASP108 |
| A | ARG151 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A1437 |
| Chain | Residue |
| A | HIS213 |
| A | SER259 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B1436 |
| Chain | Residue |
| B | ASP108 |
| B | ARG151 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B1437 |
| Chain | Residue |
| B | HIS213 |
| B | SER259 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B1438 |
| Chain | Residue |
| B | TYR373 |
| A | TYR373 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C1436 |
| Chain | Residue |
| C | ASP108 |
| C | ARG151 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C1437 |
| Chain | Residue |
| C | SER259 |
| C | HOH2141 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D1439 |
| Chain | Residue |
| D | ASP108 |
| D | ARG151 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D1440 |
| Chain | Residue |
| D | HIS213 |
| D | SER259 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D1441 |
| Chain | Residue |
| C | TYR373 |
| D | TYR373 |
| site_id | BC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD A1433 |
| Chain | Residue |
| A | PHE174 |
| A | LEU176 |
| A | SER177 |
| A | GLY182 |
| A | SER183 |
| A | TRP207 |
| A | SER209 |
| A | THR260 |
| A | ILE409 |
| A | ILE412 |
| A | ALA416 |
| A | ASN418 |
| A | ILE419 |
| A | ASN422 |
| A | COS1434 |
| A | HOH2182 |
| A | HOH2195 |
| A | HOH2196 |
| A | HOH2197 |
| A | HOH2198 |
| A | HOH2199 |
| B | GLN330 |
| C | ARG319 |
| C | GLN321 |
| C | PHE322 |
| C | LEU326 |
| C | PHE329 |
| C | LEU332 |
| C | GLU387 |
| C | TRP388 |
| C | GLY391 |
| C | HOH2203 |
| site_id | BC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE COS A1434 |
| Chain | Residue |
| A | SER183 |
| A | SER185 |
| A | TYR229 |
| A | LYS230 |
| A | TYR283 |
| A | ILE287 |
| A | LEU290 |
| A | ASN291 |
| A | ARG294 |
| A | TYR413 |
| A | GLU414 |
| A | GLY415 |
| A | ILE419 |
| A | FAD1433 |
| A | HOH2062 |
| A | HOH2185 |
| A | HOH2201 |
| A | HOH2202 |
| C | PHE322 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A1435 |
| Chain | Residue |
| A | VAL131 |
| A | PRO399 |
| A | TYR403 |
| A | HOH2203 |
| A | HOH2204 |
| site_id | BC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD B1433 |
| Chain | Residue |
| D | ARG319 |
| D | GLN321 |
| D | PHE322 |
| D | LEU326 |
| D | PHE329 |
| D | LEU332 |
| D | GLU387 |
| D | TRP388 |
| D | GLY391 |
| D | HOH2227 |
| A | GLN330 |
| B | PHE174 |
| B | LEU176 |
| B | SER177 |
| B | GLY182 |
| B | SER183 |
| B | TRP207 |
| B | SER209 |
| B | LYS252 |
| B | THR260 |
| B | ILE409 |
| B | ILE412 |
| B | ALA416 |
| B | ASN418 |
| B | ASN422 |
| B | COS1434 |
| B | HOH2181 |
| B | HOH2193 |
| B | HOH2194 |
| B | HOH2195 |
| B | HOH2196 |
| B | HOH2197 |
| B | HOH2198 |
| site_id | BC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE COS B1434 |
| Chain | Residue |
| B | SER183 |
| B | SER185 |
| B | PHE186 |
| B | TYR229 |
| B | TYR283 |
| B | ILE287 |
| B | LEU290 |
| B | ASN291 |
| B | ARG294 |
| B | TYR413 |
| B | GLU414 |
| B | GLY415 |
| B | ILE419 |
| B | FAD1433 |
| B | HOH2200 |
| B | HOH2201 |
| B | HOH2202 |
| D | PHE322 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B1435 |
| Chain | Residue |
| B | ARG256 |
| B | HOH2203 |
| B | HOH2204 |
| D | ARG256 |
| D | HOH2030 |
| D | HOH2231 |
| site_id | BC8 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD C1433 |
| Chain | Residue |
| A | ARG319 |
| A | GLN321 |
| A | PHE322 |
| A | LEU326 |
| A | PHE329 |
| A | LEU332 |
| A | GLU387 |
| A | TRP388 |
| A | GLY391 |
| A | HOH2166 |
| C | PHE174 |
| C | LEU176 |
| C | SER177 |
| C | GLY182 |
| C | SER183 |
| C | TRP207 |
| C | SER209 |
| C | THR260 |
| C | ILE409 |
| C | ILE412 |
| C | ALA416 |
| C | ASN418 |
| C | ASN422 |
| C | COS1434 |
| C | HOH2113 |
| C | HOH2226 |
| C | HOH2227 |
| C | HOH2228 |
| C | HOH2229 |
| C | HOH2230 |
| D | GLN330 |
| site_id | BC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE COS C1434 |
| Chain | Residue |
| C | SER183 |
| C | SER185 |
| C | PHE186 |
| C | TYR229 |
| C | LYS230 |
| C | TYR283 |
| C | ILE287 |
| C | ASN291 |
| C | ARG294 |
| C | TYR413 |
| C | GLU414 |
| C | GLY415 |
| C | ILE419 |
| C | FAD1433 |
| C | HOH2089 |
| C | HOH2220 |
| C | HOH2221 |
| C | HOH2231 |
| C | HOH2232 |
| C | HOH2233 |
| C | HOH2234 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C1435 |
| Chain | Residue |
| C | VAL131 |
| C | PRO399 |
| C | TYR403 |
| C | HOH2235 |
| C | HOH2236 |
| site_id | CC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD D1433 |
| Chain | Residue |
| B | ARG319 |
| B | PHE322 |
| B | LEU326 |
| B | PHE329 |
| B | LEU332 |
| B | GLU387 |
| B | TRP388 |
| B | GLY391 |
| B | HOH2165 |
| C | GLN330 |
| D | PHE174 |
| D | LEU176 |
| D | SER177 |
| D | GLY182 |
| D | SER183 |
| D | TRP207 |
| D | ILE208 |
| D | SER209 |
| D | ILE409 |
| D | ILE412 |
| D | ALA416 |
| D | ASN418 |
| D | ILE419 |
| D | ASN422 |
| D | COS1434 |
| D | HOH2241 |
| D | HOH2243 |
| D | HOH2255 |
| D | HOH2256 |
| D | HOH2257 |
| D | HOH2258 |
| D | HOH2259 |
| site_id | CC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE COS D1434 |
| Chain | Residue |
| D | SER183 |
| D | SER185 |
| D | PHE186 |
| D | TYR229 |
| D | TYR283 |
| D | ILE287 |
| D | LEU290 |
| D | ASN291 |
| D | ARG294 |
| D | ILE364 |
| D | TYR413 |
| D | GLU414 |
| D | GLY415 |
| D | ILE419 |
| D | FAD1433 |
| D | EDO1437 |
| D | HOH2097 |
| D | HOH2261 |
| D | HOH2262 |
| D | HOH2263 |
| D | HOH2264 |
| D | HOH2265 |
| D | HOH2267 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D1435 |
| Chain | Residue |
| C | LYS88 |
| D | GLN158 |
| D | TYR162 |
| D | LEU236 |
| D | ALA273 |
| D | ASN274 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D1436 |
| Chain | Residue |
| C | LYS91 |
| D | VAL237 |
| D | ASP238 |
| D | THR241 |
| D | ASN274 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D1437 |
| Chain | Residue |
| B | PHE322 |
| D | ILE419 |
| D | ASN422 |
| D | COS1434 |
| D | HOH2267 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D1438 |
| Chain | Residue |
| D | VAL131 |
| D | PRO399 |
| D | TYR403 |
| D | HOH2269 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human short-branched chain acyl-CoA dehydrogenase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 52 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human short-branched chain acyl-CoA dehydrogenase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human short-branched chain acyl-CoA dehydrogenase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9DBL1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DBL1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLY293 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | GLY293 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| C | GLY293 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| D | GLY293 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLU414 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | GLU414 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| C | GLU414 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| D | GLU414 |






