4X8B
Ergothioneine-biosynthetic sulfoxide synthase EgtB, apo form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0044875 | molecular_function | gamma-glutamyl hercynylcysteine sulfoxide synthase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052699 | biological_process | ergothioneine biosynthetic process |
| A | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0044875 | molecular_function | gamma-glutamyl hercynylcysteine sulfoxide synthase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0052699 | biological_process | ergothioneine biosynthetic process |
| B | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 501 |
| Chain | Residue |
| A | HIS200 |
| A | HOH876 |
| A | ILE297 |
| A | ARG367 |
| A | PRO368 |
| A | PRO370 |
| A | HOH825 |
| A | HOH647 |
| A | HOH692 |
| A | HOH963 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | GLN137 |
| A | TYR380 |
| A | ASN414 |
| A | TRP415 |
| A | GOL503 |
| A | HOH640 |
| A | HOH1019 |
| A | HOH801 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | GLN137 |
| A | GLU140 |
| A | GLN144 |
| A | TRP359 |
| A | PHE412 |
| A | ASN414 |
| A | GOL502 |
| A | HOH789 |
| A | HOH877 |
| A | HOH801 |
| A | HOH931 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | SER172 |
| A | ALA289 |
| A | GLY290 |
| A | TRP431 |
| A | TRP431 |
| A | HOH618 |
| A | HOH709 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | ASP416 |
| A | ARG420 |
| A | GLN422 |
| A | HOH633 |
| A | HOH678 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 506 |
| Chain | Residue |
| A | ARG87 |
| A | ARG90 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 507 |
| Chain | Residue |
| A | HOH1062 |
| A | HOH1069 |
| A | HOH1174 |
| A | HOH1281 |
| A | HOH1251 |
| A | HOH1284 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue FE A 508 |
| Chain | Residue |
| A | HIS51 |
| A | HIS134 |
| A | HIS138 |
| A | HOH622 |
| A | HOH1000 |
| A | HOH977 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue CA A 509 |
| Chain | Residue |
| A | GLN353 |
| A | MET354 |
| A | GLY356 |
| A | VAL358 |
| A | GLU360 |
| A | GLY398 |
| A | GLY399 |
| A | HOH780 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 501 |
| Chain | Residue |
| B | GLN137 |
| B | TYR380 |
| B | ASN414 |
| B | TRP415 |
| B | GOL502 |
| site_id | AD2 |
| Number of Residues | 11 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | GLN137 |
| B | GLU140 |
| B | GLN144 |
| B | TRP359 |
| B | PHE412 |
| B | ASN414 |
| B | GOL501 |
| B | HOH743 |
| B | HOH678 |
| B | HOH895 |
| B | HOH795 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | HIS200 |
| B | ILE297 |
| B | PRO370 |
| B | HOH920 |
| B | HOH746 |
| B | HOH931 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | ALA217 |
| B | ARG220 |
| B | TRP253 |
| B | PRO270 |
| B | HOH789 |
| B | HOH721 |
| B | HOH633 |
| B | HOH690 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | HOH601 |
| B | HOH830 |
| B | LEU247 |
| B | GLN251 |
| B | ARG421 |
| B | HOH704 |
| B | HOH646 |
| B | HOH913 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 506 |
| Chain | Residue |
| B | ARG87 |
| B | ARG90 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 507 |
| Chain | Residue |
| A | ASP117 |
| A | HOH810 |
| A | HOH881 |
| B | ASP267 |
| B | HOH621 |
| B | HOH690 |
| B | HOH737 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue FE B 508 |
| Chain | Residue |
| B | HIS51 |
| B | HIS134 |
| B | HIS138 |
| B | HOH833 |
| B | HOH972 |
| B | HOH977 |
| site_id | AD9 |
| Number of Residues | 8 |
| Details | binding site for residue CA B 509 |
| Chain | Residue |
| B | GLN353 |
| B | MET354 |
| B | GLY356 |
| B | VAL358 |
| B | GLU360 |
| B | GLY398 |
| B | GLY399 |
| B | HOH805 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25597398, ECO:0007744|PDB:4X8E |
| Chain | Residue | Details |
| A | HIS51 | |
| A | HIS134 | |
| A | HIS138 | |
| B | HIS51 | |
| B | HIS134 | |
| B | HIS138 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25597398, ECO:0007744|PDB:4X8D |
| Chain | Residue | Details |
| A | ARG87 | |
| A | ASP416 | |
| A | ARG420 | |
| B | ARG87 | |
| B | ASP416 | |
| B | ARG420 |
