6FNR
Ergothioneine-biosynthetic methyltransferase EgtD in complex with chlorohistidine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008276 | molecular_function | protein methyltransferase activity |
| A | 0030745 | molecular_function | dimethylhistidine N-methyltransferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0052699 | biological_process | ergothioneine biosynthetic process |
| A | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| A | 0052707 | biological_process | N-alpha,N-alpha,N-alpha-trimethyl-L-histidine biosynthesis from histidine |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008276 | molecular_function | protein methyltransferase activity |
| B | 0030745 | molecular_function | dimethylhistidine N-methyltransferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0052699 | biological_process | ergothioneine biosynthetic process |
| B | 0052704 | biological_process | ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide |
| B | 0052707 | biological_process | N-alpha,N-alpha,N-alpha-trimethyl-L-histidine biosynthesis from histidine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | ASP181 |
| A | ASP268 |
| A | HOH532 |
| A | HOH564 |
| A | HOH614 |
| A | HOH619 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | HOH525 |
| A | HOH569 |
| A | ALA15 |
| A | HOH515 |
| A | HOH518 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue DYT A 403 |
| Chain | Residue |
| A | TYR39 |
| A | TYR56 |
| A | TYR206 |
| A | GLU282 |
| A | SER284 |
| A | HOH522 |
| A | HOH554 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue PG4 A 404 |
| Chain | Residue |
| A | ASP208 |
| A | ALA209 |
| A | GLY211 |
| A | ALA215 |
| A | ARG218 |
| A | HOH501 |
| A | HOH516 |
| A | HOH588 |
| A | HOH607 |
| A | HOH682 |
| B | GLY211 |
| B | ALA215 |
| B | ARG218 |
| B | LEU234 |
| B | HOH509 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 401 |
| Chain | Residue |
| B | ALA15 |
| B | HOH531 |
| B | HOH555 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue DYT B 402 |
| Chain | Residue |
| B | TYR39 |
| B | TYR56 |
| B | ASN166 |
| B | TYR206 |
| B | GLU282 |
| B | SER284 |
| B | HOH532 |
| B | HOH552 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25251321, ECO:0000305|PubMed:25404173, ECO:0007744|PDB:4UY6, ECO:0007744|PDB:4UY7 |
| Chain | Residue | Details |
| A | TYR56 | |
| A | ASN166 | |
| A | TYR206 | |
| A | GLU282 | |
| B | TYR56 | |
| B | ASN166 | |
| B | TYR206 | |
| B | GLU282 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:25251321, ECO:0000305|PubMed:25404173 |
| Chain | Residue | Details |
| A | GLY86 | |
| A | LYS92 | |
| A | ASP113 | |
| B | GLY86 | |
| B | LYS92 | |
| B | ASP113 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:25251321, ECO:0000305|PubMed:25404173, ECO:0007744|PDB:4PIO, ECO:0007744|PDB:4PIP, ECO:0007744|PDB:4UY6 |
| Chain | Residue | Details |
| A | ASP141 | |
| B | ASP141 |
