3FCJ
Nitroalkane oxidase: mutant402N crystallized with nitroethane
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 | 34 |
Details | BINDING SITE FOR RESIDUE FAD A 500 |
Chain | Residue |
A | LEU131 |
A | SER171 |
A | LEU400 |
A | PHE401 |
A | ASN402 |
A | GLY403 |
A | GLY404 |
A | ILE406 |
A | GLY407 |
A | LEU408 |
A | HOH448 |
A | HIS133 |
A | HOH451 |
A | HOH515 |
A | NIE600 |
B | ARG304 |
B | ILE310 |
B | HIS313 |
B | VAL316 |
B | LYS375 |
B | ALA376 |
B | VAL377 |
A | SER134 |
B | GLY378 |
B | MET379 |
B | HOH445 |
B | HOH478 |
C | GLN314 |
A | GLY138 |
A | THR139 |
A | ALA140 |
A | ASN141 |
A | TRP169 |
A | PRO170 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NIE A 600 |
Chain | Residue |
A | PHE401 |
A | ASN402 |
A | FAD500 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 700 |
Chain | Residue |
A | GLU270 |
A | PHE273 |
A | GLY403 |
A | GLN412 |
A | HOH453 |
A | HOH456 |
A | HOH511 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 701 |
Chain | Residue |
A | GLN10 |
A | SER72 |
A | VAL74 |
A | GLU342 |
C | VAL2 |
site_id | AC5 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE FAD B 500 |
Chain | Residue |
A | ARG304 |
A | ILE310 |
A | HIS313 |
A | VAL316 |
A | LYS375 |
A | ALA376 |
A | VAL377 |
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 | ASN402 |
B | GLY403 |
B | GLY404 |
B | ILE406 |
B | GLY407 |
B | LEU408 |
B | ARG411 |
B | HOH447 |
B | HOH449 |
B | HOH457 |
B | NIE600 |
D | GLN314 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NIE B 600 |
Chain | Residue |
B | ASN402 |
B | FAD500 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 700 |
Chain | Residue |
B | GLU270 |
B | PHE273 |
B | GLY403 |
B | LEU408 |
B | GLN412 |
B | HOH464 |
B | HOH472 |
site_id | AC8 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE FAD C 500 |
Chain | Residue |
C | TRP169 |
C | PRO170 |
C | SER171 |
C | LEU400 |
C | PHE401 |
C | ASN402 |
C | GLY403 |
C | GLY404 |
C | ILE406 |
C | GLY407 |
C | LEU408 |
C | ARG411 |
C | HOH448 |
C | HOH460 |
C | HOH498 |
C | HOH509 |
C | NIE600 |
D | ARG304 |
D | ILE310 |
D | HIS313 |
D | VAL316 |
D | LYS375 |
D | ALA376 |
D | VAL377 |
D | GLY378 |
D | MET379 |
D | HOH441 |
A | GLN314 |
C | LEU131 |
C | HIS133 |
C | SER134 |
C | GLY138 |
C | THR139 |
C | ALA140 |
C | ASN141 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NIE C 600 |
Chain | Residue |
C | LEU99 |
C | ASN402 |
C | FAD500 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 700 |
Chain | Residue |
C | GLU270 |
C | GLY403 |
C | LEU408 |
C | GLN412 |
C | HOH468 |
C | HOH470 |
C | HOH479 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 701 |
Chain | Residue |
A | VAL2 |
C | GLN10 |
C | SER72 |
C | VAL74 |
C | GLU342 |
site_id | BC3 |
Number of Residues | 39 |
Details | BINDING SITE FOR RESIDUE FAD D 500 |
Chain | Residue |
B | GLN314 |
C | ARG304 |
C | ILE310 |
C | HIS313 |
C | VAL316 |
C | LYS375 |
C | ALA376 |
C | VAL377 |
C | GLY378 |
C | MET379 |
C | HOH453 |
C | HOH524 |
D | LEU99 |
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 | ASN402 |
D | GLY403 |
D | GLY404 |
D | ILE406 |
D | GLY407 |
D | LEU408 |
D | HOH442 |
D | HOH447 |
D | HOH448 |
D | HOH449 |
D | HOH457 |
D | HOH516 |
D | HOH531 |
D | NIE600 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NIE D 600 |
Chain | Residue |
D | LEU99 |
D | PHE273 |
D | PHE401 |
D | ASN402 |
D | FAD500 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL D 700 |
Chain | Residue |
D | HOH1 |
D | GLU270 |
D | PHE273 |
D | GLY403 |
D | LEU408 |
D | GLN412 |
D | HOH440 |
D | HOH448 |
D | HOH503 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:11867731, ECO:0000305|PubMed:12862464, ECO:0000305|PubMed:16430210 |
Chain | Residue | Details |
A | ASN402 | |
B | ASN402 | |
C | ASN402 | |
D | ASN402 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16430210, ECO:0000269|PubMed:17994768, ECO:0000269|PubMed:19926855 |
Chain | Residue | Details |
A | LEU131 | |
B | TRP169 | |
B | ARG304 | |
B | HIS313 | |
B | LYS375 | |
B | LEU400 | |
C | LEU131 | |
C | THR139 | |
C | TRP169 | |
C | ARG304 | |
C | HIS313 | |
A | THR139 | |
C | LYS375 | |
C | LEU400 | |
D | LEU131 | |
D | THR139 | |
D | TRP169 | |
D | ARG304 | |
D | HIS313 | |
D | LYS375 | |
D | LEU400 | |
A | TRP169 | |
A | ARG304 | |
A | HIS313 | |
A | LYS375 | |
A | LEU400 | |
B | LEU131 | |
B | THR139 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
A | SER276 |
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 | SER276 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
C | SER276 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
D | SER276 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
A | ASN402 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
B | ASN402 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
C | ASN402 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
D | ASN402 |
site_id | CSA9 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ivh |
Chain | Residue | Details |
A | GLY281 |