4RNU
G303 Circular Permutation of Old Yellow Enzyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE FMN A 501 |
| Chain | Residue |
| A | GLY24 |
| A | GLN213 |
| A | HIS290 |
| A | ASN293 |
| A | ARG342 |
| A | PO4502 |
| A | ASN25 |
| A | GLY47 |
| A | ARG48 |
| A | TYR75 |
| A | PRO133 |
| A | PRO134 |
| A | LEU135 |
| A | THR136 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 502 |
| Chain | Residue |
| A | HIS290 |
| A | ASN293 |
| A | TYR295 |
| A | PHE349 |
| A | FMN501 |
| A | HOH634 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE FMN B 501 |
| Chain | Residue |
| B | GLY24 |
| B | ASN25 |
| B | TYR46 |
| B | GLY47 |
| B | ARG48 |
| B | TYR75 |
| B | PRO133 |
| B | PRO134 |
| B | THR136 |
| B | GLN213 |
| B | HIS290 |
| B | ASN293 |
| B | ARG342 |
| B | PO4502 |
| B | HOH626 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 502 |
| Chain | Residue |
| B | HIS290 |
| B | ASN293 |
| B | TYR295 |
| B | PHE349 |
| B | FMN501 |
| B | HOH625 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE FMN C 501 |
| Chain | Residue |
| C | GLY24 |
| C | ASN25 |
| C | TYR46 |
| C | GLY47 |
| C | ARG48 |
| C | PRO133 |
| C | PRO134 |
| C | LEU135 |
| C | THR136 |
| C | GLN213 |
| C | HIS290 |
| C | ASN293 |
| C | ARG342 |
| C | PO4502 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 502 |
| Chain | Residue |
| C | THR136 |
| C | HIS290 |
| C | ASN293 |
| C | TYR295 |
| C | FMN501 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE FMN D 501 |
| Chain | Residue |
| D | GLY24 |
| D | ASN25 |
| D | TYR46 |
| D | GLY47 |
| D | ARG48 |
| D | PRO133 |
| D | PRO134 |
| D | LEU135 |
| D | THR136 |
| D | GLN213 |
| D | HIS290 |
| D | ASN293 |
| D | ARG342 |
| D | PO4502 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 D 502 |
| Chain | Residue |
| D | HIS290 |
| D | ASN293 |
| D | TYR295 |
| D | PHE349 |
| D | FMN501 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"9830020","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11668181","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7881908","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9830019","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11668181","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7881908","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 319 |
| Chain | Residue | Details |
| A | THR136 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS290 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN293 | electrostatic stabiliser, hydrogen bond donor |
| A | TYR295 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASN350 | hydrogen bond donor, increase acidity |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 319 |
| Chain | Residue | Details |
| B | THR136 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS290 | electrostatic stabiliser, hydrogen bond donor |
| B | ASN293 | electrostatic stabiliser, hydrogen bond donor |
| B | TYR295 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASN350 | hydrogen bond donor, increase acidity |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 319 |
| Chain | Residue | Details |
| C | THR136 | electrostatic stabiliser, hydrogen bond donor |
| C | HIS290 | electrostatic stabiliser, hydrogen bond donor |
| C | ASN293 | electrostatic stabiliser, hydrogen bond donor |
| C | TYR295 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ASN350 | hydrogen bond donor, increase acidity |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 319 |
| Chain | Residue | Details |
| D | THR136 | electrostatic stabiliser, hydrogen bond donor |
| D | HIS290 | electrostatic stabiliser, hydrogen bond donor |
| D | ASN293 | electrostatic stabiliser, hydrogen bond donor |
| D | TYR295 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | ASN350 | hydrogen bond donor, increase acidity |
