2GV8
Crystal structure of flavin-containing monooxygenase (FMO) from S.pombe and NADPH cofactor complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0071949 | molecular_function | FAD binding |
| A | 1990748 | biological_process | cellular detoxification |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016709 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0071949 | molecular_function | FAD binding |
| B | 1990748 | biological_process | cellular detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD A 500 |
| Chain | Residue |
| A | GLY13 |
| A | TRP47 |
| A | PRO83 |
| A | LEU84 |
| A | LEU88 |
| A | THR90 |
| A | ASN91 |
| A | THR92 |
| A | THR136 |
| A | ASP137 |
| A | VAL138 |
| A | GLY15 |
| A | CYS172 |
| A | ASN173 |
| A | GLY174 |
| A | TYR176 |
| A | PHE296 |
| A | PRO342 |
| A | PHE343 |
| A | NDP501 |
| A | HOH503 |
| A | HOH508 |
| A | PRO16 |
| A | HOH511 |
| A | HOH512 |
| A | HOH527 |
| A | HOH542 |
| A | HOH545 |
| A | HOH599 |
| A | HOH627 |
| A | HOH673 |
| A | SER17 |
| A | GLU38 |
| A | ARG39 |
| A | ARG40 |
| A | GLY45 |
| A | VAL46 |
| site_id | AC2 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD B 500 |
| Chain | Residue |
| B | GLY13 |
| B | GLY15 |
| B | PRO16 |
| B | SER17 |
| B | GLU38 |
| B | ARG39 |
| B | ARG40 |
| B | GLY45 |
| B | VAL46 |
| B | TRP47 |
| B | PRO83 |
| B | LEU84 |
| B | LEU88 |
| B | THR90 |
| B | ASN91 |
| B | THR92 |
| B | THR136 |
| B | ASP137 |
| B | VAL138 |
| B | CYS172 |
| B | ASN173 |
| B | GLY174 |
| B | TYR176 |
| B | PHE296 |
| B | PRO342 |
| B | PHE343 |
| B | NDP501 |
| B | HOH503 |
| B | HOH508 |
| B | HOH511 |
| B | HOH529 |
| B | HOH531 |
| B | HOH532 |
| B | HOH539 |
| B | HOH562 |
| B | HOH570 |
| B | HOH622 |
| B | HOH626 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NDP A 501 |
| Chain | Residue |
| A | TYR85 |
| A | GLN89 |
| A | ASN91 |
| A | TYR176 |
| A | GLY219 |
| A | ALA221 |
| A | SER222 |
| A | SER223 |
| A | ASP226 |
| A | SER242 |
| A | LEU244 |
| A | CYS287 |
| A | THR288 |
| A | FAD500 |
| A | HOH533 |
| A | HOH535 |
| A | HOH563 |
| A | HOH570 |
| A | HOH579 |
| A | HOH602 |
| A | HOH648 |
| A | HOH661 |
| A | HOH670 |
| A | HOH712 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NDP B 501 |
| Chain | Residue |
| B | TYR85 |
| B | GLN89 |
| B | ASN91 |
| B | TYR176 |
| B | GLY219 |
| B | ALA221 |
| B | SER222 |
| B | SER223 |
| B | ASP226 |
| B | SER242 |
| B | LEU244 |
| B | CYS287 |
| B | THR288 |
| B | GLY289 |
| B | FAD500 |
| B | HOH573 |
| B | HOH576 |
| B | HOH594 |
| B | HOH648 |
| B | HOH672 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 502 |
| Chain | Residue |
| A | TYR49 |
| A | SER51 |
| A | ARG86 |
| A | GLU206 |
| A | HOH509 |
| A | HOH653 |
| A | HOH654 |
| B | ASN48 |
| B | HOH636 |
| B | HOH641 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 502 |
| Chain | Residue |
| A | ASN48 |
| A | HOH585 |
| B | TYR49 |
| B | SER51 |
| B | ARG86 |
| B | GLU206 |
| B | HOH505 |
| B | HOH631 |
| B | HOH632 |
| B | HOH702 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16777962","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1VQW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GV8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GVC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16777962","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2GV8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b5q |
| Chain | Residue | Details |
| A | THR68 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b5q |
| Chain | Residue | Details |
| B | THR68 |
