3GXO
Structure of the Mitomycin 7-O-methyltransferase MmcR with bound Mitomycin A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008171 | molecular_function | O-methyltransferase activity |
| A | 0032259 | biological_process | methylation |
| A | 1901663 | biological_process | quinone biosynthetic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008171 | molecular_function | O-methyltransferase activity |
| B | 0032259 | biological_process | methylation |
| B | 1901663 | biological_process | quinone biosynthetic process |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0008171 | molecular_function | O-methyltransferase activity |
| C | 0032259 | biological_process | methylation |
| C | 1901663 | biological_process | quinone biosynthetic process |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0008171 | molecular_function | O-methyltransferase activity |
| D | 0032259 | biological_process | methylation |
| D | 1901663 | biological_process | quinone biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SAH A 350 |
| Chain | Residue |
| A | MSE163 |
| A | PHE241 |
| A | LYS255 |
| A | MQA351 |
| A | HOH354 |
| A | HOH361 |
| A | HOH366 |
| A | HOH377 |
| A | HOH390 |
| A | HOH399 |
| A | SER167 |
| A | GLY190 |
| A | GLY191 |
| A | GLY192 |
| A | GLU213 |
| A | ARG214 |
| A | GLY239 |
| A | ASP240 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE MQA A 351 |
| Chain | Residue |
| A | ASP110 |
| A | PHE113 |
| A | PHE159 |
| A | ALA162 |
| A | MSE163 |
| A | VAL166 |
| A | HIS256 |
| A | HIS259 |
| A | ASP260 |
| A | ASN288 |
| A | VAL301 |
| A | LEU304 |
| A | LEU308 |
| A | SAH350 |
| A | HOH371 |
| A | HOH424 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SAH D 350 |
| Chain | Residue |
| D | TRP146 |
| D | MSE163 |
| D | SER167 |
| D | GLY190 |
| D | GLY191 |
| D | GLU213 |
| D | ARG214 |
| D | GLY239 |
| D | ASP240 |
| D | PHE241 |
| D | LYS255 |
| D | TRP261 |
| D | MQA351 |
| D | HOH385 |
| D | HOH558 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MQA D 351 |
| Chain | Residue |
| D | PHE113 |
| D | PHE159 |
| D | ALA162 |
| D | HIS256 |
| D | HIS259 |
| D | ASP260 |
| D | ASN288 |
| D | LEU308 |
| D | SAH350 |
| D | HOH397 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA D 352 |
| Chain | Residue |
| D | GLU20 |
| D | ASP24 |
| D | HOH405 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SAH C 350 |
| Chain | Residue |
| C | MSE163 |
| C | SER167 |
| C | GLY190 |
| C | GLY191 |
| C | GLY192 |
| C | GLU213 |
| C | ARG214 |
| C | VAL217 |
| C | ASP240 |
| C | PHE241 |
| C | LYS255 |
| C | MQA351 |
| C | HOH364 |
| C | HOH381 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA D 353 |
| Chain | Residue |
| D | GLU134 |
| D | ASP262 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MQA C 351 |
| Chain | Residue |
| C | PHE113 |
| C | PHE159 |
| C | ALA162 |
| C | MSE163 |
| C | VAL166 |
| C | HIS256 |
| C | HIS259 |
| C | ASP260 |
| C | ASN288 |
| C | LEU304 |
| C | LEU308 |
| C | SAH350 |
| C | HOH372 |
| C | HOH467 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SAH B 350 |
| Chain | Residue |
| B | ASP240 |
| B | PHE241 |
| B | LYS255 |
| B | HIS256 |
| B | MQA351 |
| B | HOH377 |
| B | HOH380 |
| B | HOH384 |
| B | HOH573 |
| B | MSE163 |
| B | SER167 |
| B | GLY190 |
| B | GLY191 |
| B | GLY192 |
| B | GLU213 |
| B | ARG214 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MQA B 351 |
| Chain | Residue |
| B | ASP110 |
| B | PHE113 |
| B | PHE159 |
| B | ALA162 |
| B | MSE163 |
| B | HIS256 |
| B | HIS259 |
| B | ASP260 |
| B | ASN288 |
| B | LEU304 |
| B | LEU308 |
| B | SAH350 |
| B | HOH381 |
| B | HOH456 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:21538548 |
| Chain | Residue | Details |
| A | HIS259 | |
| D | HIS259 | |
| C | HIS259 | |
| B | HIS259 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21538548 |
| Chain | Residue | Details |
| A | SER167 | |
| D | ASP240 | |
| D | LYS255 | |
| D | ASN288 | |
| C | SER167 | |
| C | GLY190 | |
| C | GLU213 | |
| C | ASP240 | |
| C | LYS255 | |
| C | ASN288 | |
| B | SER167 | |
| A | GLY190 | |
| B | GLY190 | |
| B | GLU213 | |
| B | ASP240 | |
| B | LYS255 | |
| B | ASN288 | |
| A | GLU213 | |
| A | ASP240 | |
| A | LYS255 | |
| A | ASN288 | |
| D | SER167 | |
| D | GLY190 | |
| D | GLU213 |
