3SWO
Crystal structure of a glutaryl-coa dehydrogenase from mycobacterium smegmatis in complex with FADH2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000062 | molecular_function | fatty-acyl-CoA binding |
| A | 0004361 | molecular_function | glutaryl-CoA dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| A | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000062 | molecular_function | fatty-acyl-CoA binding |
| B | 0004361 | molecular_function | glutaryl-CoA dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| B | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0000062 | molecular_function | fatty-acyl-CoA binding |
| C | 0004361 | molecular_function | glutaryl-CoA dehydrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| C | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0000062 | molecular_function | fatty-acyl-CoA binding |
| D | 0004361 | molecular_function | glutaryl-CoA dehydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| D | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FDA A 500 |
| Chain | Residue |
| A | PHE141 |
| A | SER370 |
| A | THR373 |
| A | TYR374 |
| A | THR377 |
| A | GLU379 |
| A | MET380 |
| A | PHE395 |
| A | HOH429 |
| A | HOH446 |
| A | HOH457 |
| A | LEU143 |
| A | EDO503 |
| A | HOH521 |
| A | HOH534 |
| A | HOH1386 |
| C | GLN291 |
| D | ARG280 |
| D | VAL282 |
| D | PHE283 |
| D | LEU287 |
| D | TYR290 |
| A | THR144 |
| D | THR348 |
| D | LEU349 |
| D | GLY352 |
| D | HOH523 |
| D | HOH527 |
| A | GLY149 |
| A | SER150 |
| A | TRP174 |
| A | ILE175 |
| A | THR176 |
| A | LEU217 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 501 |
| Chain | Residue |
| A | ARG344 |
| A | ALA365 |
| A | GLU369 |
| D | ARG344 |
| D | ALA365 |
| D | GLU369 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | ARG102 |
| A | VAL107 |
| A | LEU111 |
| A | THR176 |
| A | TYR374 |
| A | GLU375 |
| A | FDA500 |
| A | HOH1386 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | GLY149 |
| A | SER150 |
| A | LEU248 |
| A | LEU251 |
| A | ARG255 |
| A | GLU375 |
| A | GLY376 |
| A | HOH841 |
| A | HOH1247 |
| site_id | AC5 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FDA B 500 |
| Chain | Residue |
| B | PHE141 |
| B | LEU143 |
| B | THR144 |
| B | GLY149 |
| B | SER150 |
| B | TRP174 |
| B | ILE175 |
| B | THR176 |
| B | LEU217 |
| B | SER370 |
| B | THR373 |
| B | TYR374 |
| B | THR377 |
| B | GLU379 |
| B | MET380 |
| B | PHE395 |
| B | HOH406 |
| B | HOH414 |
| B | HOH428 |
| B | HOH431 |
| B | HOH436 |
| B | HOH452 |
| B | EDO503 |
| B | HOH941 |
| C | ARG280 |
| C | VAL282 |
| C | PHE283 |
| C | LEU287 |
| C | TYR290 |
| C | THR348 |
| C | LEU349 |
| C | GLY352 |
| C | HOH436 |
| C | HOH1137 |
| D | GLN291 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 501 |
| Chain | Residue |
| B | ARG344 |
| B | GLU369 |
| C | ARG344 |
| C | ALA365 |
| C | GLU369 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 503 |
| Chain | Residue |
| B | VAL107 |
| B | THR176 |
| B | TYR374 |
| B | GLU375 |
| B | FDA500 |
| B | ARG102 |
| B | SER103 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO B 505 |
| Chain | Residue |
| B | SER150 |
| B | LEU248 |
| B | LEU251 |
| B | ARG255 |
| B | GLU375 |
| B | GLY376 |
| B | MET380 |
| B | HOH725 |
| B | HOH941 |
| B | HOH1919 |
| site_id | AC9 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FDA C 500 |
| Chain | Residue |
| A | GLN291 |
| B | ARG280 |
| B | VAL282 |
| B | PHE283 |
| B | LEU287 |
| B | TYR290 |
| B | THR348 |
| B | LEU349 |
| B | GLY352 |
| B | HOH424 |
| B | HOH496 |
| C | PHE141 |
| C | LEU143 |
| C | THR144 |
| C | GLY149 |
| C | SER150 |
| C | TRP174 |
| C | ILE175 |
| C | THR176 |
| C | LEU217 |
| C | SER370 |
| C | THR373 |
| C | TYR374 |
| C | THR377 |
| C | GLU379 |
| C | MET380 |
| C | PHE395 |
| C | HOH401 |
| C | HOH419 |
| C | HOH434 |
| C | HOH464 |
| C | HOH472 |
| C | HOH478 |
| C | EDO503 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO C 503 |
| Chain | Residue |
| C | ARG102 |
| C | SER106 |
| C | VAL107 |
| C | LEU111 |
| C | THR176 |
| C | TYR374 |
| C | GLU375 |
| C | HOH401 |
| C | FDA500 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 505 |
| Chain | Residue |
| C | LEU248 |
| C | LEU251 |
| C | ARG255 |
| C | GLU375 |
| C | GLY376 |
| C | HOH580 |
| C | HOH1110 |
| site_id | BC3 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FDA D 500 |
| Chain | Residue |
| A | ARG280 |
| A | VAL282 |
| A | PHE283 |
| A | LEU287 |
| A | TYR290 |
| A | THR348 |
| A | LEU349 |
| A | GLY352 |
| A | HOH471 |
| A | HOH547 |
| B | GLN291 |
| D | PHE141 |
| D | LEU143 |
| D | THR144 |
| D | GLY149 |
| D | SER150 |
| D | TRP174 |
| D | ILE175 |
| D | THR176 |
| D | LEU217 |
| D | SER370 |
| D | THR373 |
| D | TYR374 |
| D | THR377 |
| D | GLU379 |
| D | MET380 |
| D | PHE395 |
| D | HOH425 |
| D | HOH428 |
| D | HOH459 |
| D | HOH461 |
| D | HOH472 |
| D | EDO503 |
| D | HOH1132 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 503 |
| Chain | Residue |
| D | ARG102 |
| D | SER103 |
| D | VAL107 |
| D | THR176 |
| D | TYR374 |
| D | GLU375 |
| D | FDA500 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO D 505 |
| Chain | Residue |
| D | SER150 |
| D | PRO152 |
| D | LEU248 |
| D | LEU251 |
| D | ARG255 |
| D | GLU375 |
| D | GLY376 |
| D | HOH677 |
| D | HOH1107 |
