3II9
Crystal structure of glutaryl-coa dehydrogenase from Burkholderia pseudomallei at 1.73 Angstrom
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
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 | 0046872 | molecular_function | metal ion binding |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
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 | 0046872 | molecular_function | metal ion binding |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
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 | 0046872 | molecular_function | metal ion binding |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
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 | 0046872 | molecular_function | metal ion binding |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG A 396 |
Chain | Residue |
A | VAL214 |
A | HOH433 |
C | PHE45 |
C | ALA361 |
C | ARG362 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 397 |
Chain | Residue |
A | HOH492 |
A | HOH509 |
A | HOH450 |
A | HOH463 |
A | HOH472 |
A | HOH480 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PGE A 398 |
Chain | Residue |
A | LYS36 |
A | ARG40 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PG4 B 396 |
Chain | Residue |
B | PHE6 |
B | TRP8 |
B | ASP9 |
B | ARG273 |
B | HOH1101 |
C | PRO158 |
C | GLY159 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PG4 B 397 |
Chain | Residue |
B | ARG97 |
B | SER98 |
B | PHE136 |
B | LEU138 |
B | THR139 |
B | VAL370 |
B | HOH408 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL B 398 |
Chain | Residue |
B | ALA19 |
B | ARG315 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PGE C 396 |
Chain | Residue |
C | GLY35 |
C | LYS36 |
C | ARG40 |
C | HOH991 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG C 397 |
Chain | Residue |
C | GLU121 |
C | LYS122 |
C | PRO125 |
C | LYS126 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 398 |
Chain | Residue |
C | LEU205 |
C | HOH519 |
C | HOH1007 |
C | HOH1036 |
C | HOH1123 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL C 399 |
Chain | Residue |
C | SER98 |
C | TYR373 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG C 400 |
Chain | Residue |
C | HOH963 |
C | HOH964 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PG4 C 401 |
Chain | Residue |
C | HIS7 |
C | TRP8 |
C | ASP9 |
C | ARG273 |
D | GLN388 |
D | THR389 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL D 396 |
Chain | Residue |
D | LYS36 |
D | ARG40 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG D 398 |
Chain | Residue |
C | ALA387 |
C | GLN388 |
D | ARG273 |
D | LEU277 |
D | PEG399 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL D 397 |
Chain | Residue |
D | VAL151 |
D | SER164 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG D 399 |
Chain | Residue |
D | TRP8 |
D | ASP9 |
D | PEG398 |
site_id | BC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG D 400 |
Chain | Residue |
D | HOH459 |
Functional Information from PROSITE/UniProt
site_id | PS00073 |
Number of Residues | 20 |
Details | ACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. DmLGGnGIsdEfgvaRhlvN |
Chain | Residue | Details |
A | ASP347-ASN366 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
A | ALA253 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
B | ALA253 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
C | ALA253 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
D | ALA253 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
A | GLU374 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
B | GLU374 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
C | GLU374 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
D | GLU374 |