3MPI
Structure of the glutaryl-coenzyme A dehydrogenase glutaryl-CoA complex
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 |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
C | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD A 400 |
Chain | Residue |
A | PHE126 |
A | GLN273 |
A | PHE274 |
A | PHE281 |
A | ASN284 |
A | ARG340 |
A | ILE341 |
A | GLY343 |
A | ALA344 |
A | TYR345 |
A | MET365 |
A | ILE128 |
A | VAL366 |
A | SER369 |
A | ASN371 |
A | MET375 |
A | GRA402 |
A | HOH407 |
A | HOH418 |
A | HOH450 |
A | HOH469 |
A | HOH501 |
A | THR129 |
A | HOH551 |
B | GLN282 |
A | GLY134 |
A | SER135 |
A | TRP159 |
A | ILE160 |
A | SER161 |
A | ARG271 |
site_id | AC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE GRA A 402 |
Chain | Residue |
A | ARG87 |
A | ASN91 |
A | PHE126 |
A | SER135 |
A | VAL137 |
A | SER181 |
A | PHE239 |
A | ASN243 |
A | ARG246 |
A | PHE274 |
A | ASN315 |
A | VAL366 |
A | GLU367 |
A | GLY368 |
A | ARG385 |
A | ARG389 |
A | FAD400 |
A | HOH403 |
A | HOH440 |
A | HOH485 |
A | HOH531 |
A | HOH540 |
A | HOH552 |
C | LYS22 |
C | LYS23 |
site_id | AC3 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD B 400 |
Chain | Residue |
A | GLN282 |
B | PHE126 |
B | ILE128 |
B | THR129 |
B | GLY134 |
B | SER135 |
B | TRP159 |
B | ILE160 |
B | SER161 |
B | LYS204 |
B | ARG271 |
B | GLN273 |
B | PHE274 |
B | PHE281 |
B | ASN284 |
B | ARG340 |
B | ILE341 |
B | GLY343 |
B | ALA344 |
B | TYR345 |
B | MET365 |
B | VAL366 |
B | GLU367 |
B | SER369 |
B | ASN371 |
B | GRA402 |
B | HOH409 |
B | HOH439 |
site_id | AC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE GRA B 402 |
Chain | Residue |
B | ARG385 |
B | ARG389 |
B | FAD400 |
B | HOH405 |
B | HOH526 |
D | ASP218 |
B | ARG87 |
B | ASN91 |
B | PHE126 |
B | SER135 |
B | VAL137 |
B | SER181 |
B | ARG236 |
B | PHE239 |
B | ASN243 |
B | ARG246 |
B | PHE274 |
B | ASN315 |
B | VAL366 |
B | GLU367 |
B | GLY368 |
site_id | AC5 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD C 400 |
Chain | Residue |
C | PHE126 |
C | ILE128 |
C | THR129 |
C | GLY134 |
C | SER135 |
C | TRP159 |
C | ILE160 |
C | SER161 |
C | ARG271 |
C | GLN273 |
C | PHE274 |
C | ILE278 |
C | PHE281 |
C | ASN284 |
C | ARG340 |
C | ILE341 |
C | GLY343 |
C | ALA344 |
C | TYR345 |
C | MET365 |
C | VAL366 |
C | SER369 |
C | ASN371 |
C | MET375 |
C | GRA402 |
C | HOH404 |
C | HOH421 |
C | HOH430 |
C | HOH431 |
C | HOH518 |
C | HOH542 |
D | GLN282 |
site_id | AC6 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE GRA C 402 |
Chain | Residue |
A | LYS23 |
C | ARG87 |
C | ASN91 |
C | PHE126 |
C | SER135 |
C | VAL137 |
C | SER181 |
C | ALA235 |
C | PHE239 |
C | ASN243 |
C | ARG246 |
C | PHE274 |
C | ASN315 |
C | VAL366 |
C | GLU367 |
C | GLY368 |
C | ARG385 |
C | ARG389 |
C | FAD400 |
C | HOH407 |
C | HOH409 |
C | HOH450 |
C | HOH453 |
C | HOH491 |
C | HOH519 |
site_id | AC7 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD D 400 |
Chain | Residue |
C | GLN282 |
D | PHE126 |
D | ILE128 |
D | THR129 |
D | GLY134 |
D | SER135 |
D | TRP159 |
D | SER161 |
D | ARG271 |
D | GLN273 |
D | PHE274 |
D | PHE281 |
D | ASN284 |
D | ARG340 |
D | ILE341 |
D | GLY343 |
D | ALA344 |
D | TYR345 |
D | MET365 |
D | VAL366 |
D | GLU367 |
D | SER369 |
D | ASN371 |
D | GRA402 |
D | HOH409 |
D | HOH413 |
D | HOH436 |
D | HOH451 |
D | HOH494 |
site_id | AC8 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE GRA D 402 |
Chain | Residue |
D | ARG87 |
D | ASN91 |
D | SER135 |
D | VAL137 |
D | SER181 |
D | PHE239 |
D | ASN243 |
D | ARG246 |
D | PHE274 |
D | ASN315 |
D | VAL366 |
D | GLU367 |
D | GLY368 |
D | ARG385 |
D | ARG389 |
D | FAD400 |
D | HOH424 |
D | HOH438 |
D | HOH447 |
D | HOH452 |
D | HOH462 |
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 | 4 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 80 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"20486657","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |