3D9F
Nitroalkane oxidase: active site mutant S276A crystallized with 1-nitrohexane
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 | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| A | 0046359 | biological_process | butyrate catabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0052664 | molecular_function | nitroalkane oxidase activity |
| A | 0071949 | molecular_function | FAD binding |
| A | 0098754 | biological_process | detoxification |
| 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 | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| B | 0046359 | biological_process | butyrate catabolic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0052664 | molecular_function | nitroalkane oxidase activity |
| B | 0071949 | molecular_function | FAD binding |
| B | 0098754 | biological_process | detoxification |
| 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 | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| C | 0046359 | biological_process | butyrate catabolic process |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0052664 | molecular_function | nitroalkane oxidase activity |
| C | 0071949 | molecular_function | FAD binding |
| C | 0098754 | biological_process | detoxification |
| 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 | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| D | 0046359 | biological_process | butyrate catabolic process |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0052664 | molecular_function | nitroalkane oxidase activity |
| D | 0071949 | molecular_function | FAD binding |
| D | 0098754 | biological_process | detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD A 500 |
| Chain | Residue |
| A | LEU99 |
| A | PRO170 |
| A | SER171 |
| A | LEU400 |
| A | PHE401 |
| A | ASP402 |
| A | GLY403 |
| A | GLY404 |
| A | ILE406 |
| A | GLY407 |
| B | ARG304 |
| A | LEU131 |
| B | ILE310 |
| B | HIS313 |
| B | LYS375 |
| B | ALA376 |
| B | GLY378 |
| B | MET379 |
| C | GLN314 |
| A | HIS133 |
| A | SER134 |
| A | GLY138 |
| A | THR139 |
| A | ALA140 |
| A | ASN141 |
| A | TRP169 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE N6C A 600 |
| Chain | Residue |
| A | LEU99 |
| A | PHE273 |
| A | PHE401 |
| A | ASP402 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD B 500 |
| Chain | Residue |
| A | ARG304 |
| A | ILE310 |
| A | HIS313 |
| A | LYS375 |
| A | ALA376 |
| A | GLY378 |
| A | MET379 |
| B | LEU131 |
| B | HIS133 |
| B | SER134 |
| B | GLY138 |
| B | THR139 |
| B | ALA140 |
| B | ASN141 |
| B | TRP169 |
| B | PRO170 |
| B | SER171 |
| B | LEU400 |
| B | PHE401 |
| B | ASP402 |
| B | GLY403 |
| B | GLY404 |
| B | ILE406 |
| B | GLY407 |
| B | LEU408 |
| D | GLN314 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE N6C B 600 |
| Chain | Residue |
| B | LEU99 |
| B | PHE273 |
| B | PHE401 |
| B | ASP402 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD C 500 |
| Chain | Residue |
| A | GLN314 |
| C | LEU131 |
| C | HIS133 |
| C | SER134 |
| C | GLY138 |
| C | THR139 |
| C | ALA140 |
| C | ASN141 |
| C | TRP169 |
| C | PRO170 |
| C | SER171 |
| C | LEU400 |
| C | PHE401 |
| C | ASP402 |
| C | GLY403 |
| C | GLY404 |
| C | ILE406 |
| C | GLY407 |
| C | ARG411 |
| D | ARG304 |
| D | ILE310 |
| D | HIS313 |
| D | LYS375 |
| D | ALA376 |
| D | GLY378 |
| D | MET379 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE N6C C 600 |
| Chain | Residue |
| C | LEU99 |
| C | PHE273 |
| C | ALA276 |
| C | PHE401 |
| C | ASP402 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD D 500 |
| Chain | Residue |
| D | LEU131 |
| D | HIS133 |
| D | SER134 |
| D | GLY138 |
| D | THR139 |
| D | ALA140 |
| D | ASN141 |
| D | TRP169 |
| D | PRO170 |
| D | SER171 |
| D | LEU400 |
| D | PHE401 |
| D | ASP402 |
| D | GLY403 |
| D | GLY404 |
| D | ILE406 |
| D | GLY407 |
| D | LEU408 |
| B | GLN314 |
| C | ARG304 |
| C | ILE310 |
| C | HIS313 |
| C | LYS375 |
| C | ALA376 |
| C | GLY378 |
| C | MET379 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE N6C D 600 |
| Chain | Residue |
| D | LEU99 |
| D | PHE273 |
| D | PHE401 |
| D | ASP402 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 700 |
| Chain | Residue |
| A | GLU270 |
| A | PHE273 |
| A | GLY403 |
| A | ARG409 |
| A | GLN412 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 701 |
| Chain | Residue |
| C | GLN10 |
| C | SER72 |
| C | GLU342 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 700 |
| Chain | Residue |
| B | GLU270 |
| B | PHE273 |
| B | GLY403 |
| B | LEU408 |
| B | GLN412 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL D 701 |
| Chain | Residue |
| D | GLN10 |
| D | SER72 |
| D | GLU342 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 700 |
| Chain | Residue |
| C | GLU270 |
| C | PHE273 |
| C | GLY403 |
| C | LEU408 |
| C | ARG409 |
| C | GLN412 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 701 |
| Chain | Residue |
| A | GLN10 |
| A | SER72 |
| A | GLU342 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 700 |
| Chain | Residue |
| D | GLU270 |
| D | GLY403 |
| D | LEU408 |
| D | GLN412 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 701 |
| Chain | Residue |
| B | GLN10 |
| B | SER72 |
| B | GLU342 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11867731","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12862464","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16430210","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 68 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16430210","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17994768","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19926855","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | ALA276 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | GLY281 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| C | GLY281 |
| site_id | CSA12 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| D | GLY281 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | ALA276 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| C | ALA276 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| D | ALA276 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | ASP402 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | ASP402 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| C | ASP402 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| D | ASP402 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLY281 |
