4RNX
K154 Circular Permutation of Old Yellow Enzyme
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN A 501 |
| Chain | Residue |
| A | HIS40 |
| A | PRO283 |
| A | LEU284 |
| A | THR285 |
| A | GLY320 |
| A | GLN362 |
| A | HOH623 |
| A | HOH704 |
| A | HOH795 |
| A | HOH950 |
| A | HOH957 |
| A | ASN43 |
| A | ARG92 |
| A | GLY173 |
| A | ASN174 |
| A | GLY196 |
| A | ARG197 |
| A | PHE223 |
| A | PRO282 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 502 |
| Chain | Residue |
| A | ASN28 |
| A | GLU339 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | ALA228 |
| A | ASP233 |
| B | TRP300 |
| B | HOH630 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | HIS229 |
| A | ASP233 |
| A | HOH986 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | ASP233 |
| A | GLU239 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN B 501 |
| Chain | Residue |
| B | HIS40 |
| B | ASN43 |
| B | ARG92 |
| B | PRO144 |
| B | ASN174 |
| B | GLY196 |
| B | ARG197 |
| B | PHE223 |
| B | PRO282 |
| B | PRO283 |
| B | LEU284 |
| B | THR285 |
| B | GLY320 |
| B | GLN362 |
| B | HOH634 |
| B | HOH667 |
| B | HOH737 |
| B | HOH964 |
| B | HOH1072 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 502 |
| Chain | Residue |
| B | TYR162 |
| B | ARG171 |
| B | HOH785 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 503 |
| Chain | Residue |
| B | HIS229 |
| B | ASP233 |
| B | HOH935 |
| B | HOH1167 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| 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 | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11668181","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7881908","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| 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 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 319 |
| Chain | Residue | Details |
| A | HIS40 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN43 | electrostatic stabiliser, hydrogen bond donor |
| A | TYR45 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASN100 | hydrogen bond donor, increase acidity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 319 |
| Chain | Residue | Details |
| B | HIS40 | electrostatic stabiliser, hydrogen bond donor |
| B | ASN43 | electrostatic stabiliser, hydrogen bond donor |
| B | TYR45 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASN100 | hydrogen bond donor, increase acidity |
