3MPJ
Structure of the glutaryl-coenzyme A dehydrogenase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
E | 0000166 | molecular_function | nucleotide binding |
E | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
F | 0000166 | molecular_function | nucleotide binding |
F | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
G | 0000166 | molecular_function | nucleotide binding |
G | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE FAD A 400 |
Chain | Residue |
A | MET92 |
A | LYS204 |
A | MET365 |
A | VAL366 |
A | GLU367 |
A | SER369 |
A | ASN371 |
A | ILE372 |
A | MET375 |
A | HOH7003 |
A | HOH7004 |
A | PHE126 |
A | HOH7050 |
A | HOH7182 |
A | HOH7236 |
A | HOH7286 |
A | HOH7290 |
B | ARG271 |
B | GLN273 |
B | PHE274 |
B | ILE278 |
B | PHE281 |
A | ILE128 |
B | GLN282 |
B | ASN284 |
B | ARG340 |
B | ILE341 |
B | GLY343 |
B | ALA344 |
B | HOH7079 |
A | THR129 |
A | GLY134 |
A | SER135 |
A | TRP159 |
A | ILE160 |
A | SER161 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 401 |
Chain | Residue |
A | ASN35 |
A | LYS204 |
A | HIS208 |
A | HOH8012 |
site_id | AC3 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD B 400 |
Chain | Residue |
A | ARG271 |
A | GLN273 |
A | PHE274 |
A | ILE278 |
A | PHE281 |
A | GLN282 |
A | ASN284 |
A | ARG340 |
A | ILE341 |
A | GLY343 |
A | ALA344 |
A | TYR345 |
B | MET92 |
B | PHE126 |
B | ILE128 |
B | THR129 |
B | GLY134 |
B | SER135 |
B | TRP159 |
B | ILE160 |
B | SER161 |
B | LYS204 |
B | MET365 |
B | VAL366 |
B | GLU367 |
B | SER369 |
B | ASN371 |
B | MET375 |
B | HOH7006 |
B | HOH7011 |
B | HOH7012 |
B | HOH7021 |
B | HOH7080 |
B | HOH7129 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 401 |
Chain | Residue |
B | ASN35 |
B | LYS204 |
B | HIS208 |
B | HOH7361 |
site_id | AC5 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD D 400 |
Chain | Residue |
E | ARG271 |
E | GLN273 |
E | PHE274 |
E | PHE281 |
E | ASN284 |
E | ARG340 |
E | ILE341 |
E | GLY343 |
E | ALA344 |
E | TYR345 |
G | GLN282 |
D | PHE126 |
D | ILE128 |
D | THR129 |
D | GLY134 |
D | SER135 |
D | TRP159 |
D | ILE160 |
D | SER161 |
D | MET365 |
D | VAL366 |
D | GLU367 |
D | SER369 |
D | ASN371 |
D | MET375 |
D | HOH7422 |
D | HOH7424 |
D | HOH7436 |
D | HOH7481 |
D | HOH7586 |
D | HOH7689 |
D | HOH7981 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL D 401 |
Chain | Residue |
D | LYS204 |
D | HIS208 |
site_id | AC7 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD E 400 |
Chain | Residue |
D | ARG271 |
D | GLN273 |
D | PHE274 |
D | PHE281 |
D | ASN284 |
D | ARG340 |
D | ILE341 |
D | GLY343 |
D | ALA344 |
E | MET92 |
E | PHE126 |
E | ILE128 |
E | THR129 |
E | GLY134 |
E | SER135 |
E | TRP159 |
E | SER161 |
E | MET365 |
E | VAL366 |
E | GLU367 |
E | SER369 |
E | ASN371 |
E | MET375 |
E | HOH7692 |
E | HOH7693 |
E | HOH7849 |
E | HOH7973 |
F | GLN282 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL E 401 |
Chain | Residue |
E | ASN35 |
E | LYS204 |
E | HIS208 |
site_id | AC9 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD F 400 |
Chain | Residue |
E | GLN282 |
F | MET92 |
F | PHE126 |
F | ILE128 |
F | THR129 |
F | GLY134 |
F | SER135 |
F | TRP159 |
F | SER161 |
F | MET365 |
F | VAL366 |
F | GLU367 |
F | SER369 |
F | ASN371 |
F | MET375 |
F | HOH7403 |
F | HOH7404 |
F | HOH7421 |
F | HOH7551 |
F | HOH7705 |
G | ARG271 |
G | GLN273 |
G | PHE274 |
G | PHE281 |
G | ASN284 |
G | ARG340 |
G | ILE341 |
G | GLY343 |
G | ALA344 |
G | HOH7405 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL F 401 |
Chain | Residue |
F | ASN35 |
F | LYS204 |
F | HIS208 |
F | HOH7527 |
site_id | BC2 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD G 400 |
Chain | Residue |
D | GLN282 |
F | ARG271 |
F | GLN273 |
F | PHE274 |
F | PHE281 |
F | ASN284 |
F | ARG340 |
F | ILE341 |
F | GLY343 |
F | ALA344 |
F | HOH7433 |
G | MET92 |
G | PHE126 |
G | ILE128 |
G | THR129 |
G | GLY134 |
G | SER135 |
G | TRP159 |
G | SER161 |
G | MET365 |
G | VAL366 |
G | GLU367 |
G | SER369 |
G | ASN371 |
G | MET375 |
G | HOH7406 |
G | HOH7445 |
G | HOH7533 |
G | HOH7593 |
G | HOH7604 |
G | HOH7653 |
G | HOH7976 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL G 401 |
Chain | Residue |
G | LYS204 |
G | HIS208 |
Functional Information from PROSITE/UniProt
site_id | PS00072 |
Number of Residues | 13 |
Details | ACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. GITEpdAGSDvmA |
Chain | Residue | Details |
A | GLY127-ALA139 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 120 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"20486657","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |