2FON
X-ray crystal structure of LeACX1, an acyl-CoA oxidase from Lycopersicon esculentum (tomato)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003997 | molecular_function | acyl-CoA oxidase activity |
A | 0005777 | cellular_component | peroxisome |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006635 | biological_process | fatty acid beta-oxidation |
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 |
A | 0071949 | molecular_function | FAD binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003997 | molecular_function | acyl-CoA oxidase activity |
B | 0005777 | cellular_component | peroxisome |
B | 0006629 | biological_process | lipid metabolic process |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006635 | biological_process | fatty acid beta-oxidation |
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 |
B | 0071949 | molecular_function | FAD binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003997 | molecular_function | acyl-CoA oxidase activity |
C | 0005777 | cellular_component | peroxisome |
C | 0006629 | biological_process | lipid metabolic process |
C | 0006631 | biological_process | fatty acid metabolic process |
C | 0006635 | biological_process | fatty acid beta-oxidation |
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 |
C | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE FAD A 1000 |
Chain | Residue |
A | LEU101 |
A | ASN239 |
A | PRO419 |
A | THR422 |
A | TYR423 |
A | ASP426 |
A | VAL429 |
A | LEU432 |
B | ARG310 |
B | GLN312 |
B | PHE313 |
A | TYR135 |
B | VAL324 |
B | TYR327 |
B | THR329 |
B | GLN330 |
B | ARG333 |
B | LEU398 |
B | GLY401 |
A | GLN137 |
A | THR138 |
A | GLY143 |
A | SER144 |
A | TRP175 |
A | PRO176 |
A | GLY177 |
site_id | AC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE FAD B 2000 |
Chain | Residue |
A | ARG310 |
A | PHE313 |
A | VAL324 |
A | TYR327 |
A | THR329 |
A | GLN330 |
A | ARG333 |
A | LEU398 |
A | GLY400 |
A | GLY401 |
B | LEU101 |
B | TYR135 |
B | GLN137 |
B | THR138 |
B | GLY143 |
B | SER144 |
B | TRP175 |
B | PRO176 |
B | GLY177 |
B | PRO419 |
B | THR422 |
B | TYR423 |
B | ASP426 |
B | VAL429 |
B | LEU432 |
site_id | AC3 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE FAD C 3000 |
Chain | Residue |
C | LEU101 |
C | TYR135 |
C | GLN137 |
C | THR138 |
C | GLY143 |
C | SER144 |
C | TRP175 |
C | PRO176 |
C | GLY177 |
C | ASN239 |
C | ARG310 |
C | GLN312 |
C | PHE313 |
C | VAL324 |
C | TYR327 |
C | GLN330 |
C | ARG333 |
C | LEU398 |
C | GLY400 |
C | GLY401 |
C | TYR404 |
C | PRO419 |
C | THR422 |
C | ASP426 |
C | VAL428 |
C | VAL429 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
A | VAL284 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
B | VAL284 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
C | VAL284 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
A | GLU424 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
B | GLU424 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
C | GLU424 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
A | SER297 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
B | SER297 |
site_id | CSA9 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
C | SER297 |