6IX8
The structure of LepI C52A in complex with SAM and its substrate analogue
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008171 | molecular_function | O-methyltransferase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0018130 | biological_process | obsolete heterocycle biosynthetic process |
A | 0032259 | biological_process | methylation |
A | 0044550 | biological_process | secondary metabolite biosynthetic process |
A | 1901362 | biological_process | organic cyclic compound biosynthetic process |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0008171 | molecular_function | O-methyltransferase activity |
B | 0016740 | molecular_function | transferase activity |
B | 0018130 | biological_process | obsolete heterocycle biosynthetic process |
B | 0032259 | biological_process | methylation |
B | 0044550 | biological_process | secondary metabolite biosynthetic process |
B | 1901362 | biological_process | organic cyclic compound biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | binding site for residue SAM A 401 |
Chain | Residue |
A | GLY227 |
A | HIS277 |
A | ARG291 |
A | LEU292 |
A | HOH515 |
A | HOH594 |
A | HOH604 |
A | HOH618 |
A | HOH638 |
A | HOH685 |
A | HOH697 |
A | GLY228 |
A | HOH704 |
A | GLY229 |
A | ASP252 |
A | LEU253 |
A | VAL256 |
A | HIS274 |
A | ASN275 |
A | PHE276 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue CL A 402 |
Chain | Residue |
A | TYR241 |
A | ASN243 |
A | GLN244 |
B | THR278 |
B | PRO279 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue CL A 403 |
Chain | Residue |
A | LYS329 |
A | GLY330 |
A | ALA331 |
B | ARG97 |
B | GLN107 |
B | HOH647 |
B | HOH694 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue CL A 404 |
Chain | Residue |
A | ARG247 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue CL A 405 |
Chain | Residue |
A | SER115 |
A | SER116 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue NA A 406 |
Chain | Residue |
A | GLY330 |
A | ALA331 |
A | HOH662 |
B | HOH647 |
B | HOH795 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue NA A 407 |
Chain | Residue |
A | HOH775 |
A | HOH847 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue B3O A 408 |
Chain | Residue |
A | HIS133 |
A | LEU138 |
A | CYS175 |
A | PHE189 |
A | ARG197 |
A | ARG295 |
A | ASP296 |
A | ILE342 |
B | MET45 |
B | LEU49 |
site_id | AC9 |
Number of Residues | 20 |
Details | binding site for residue SAM B 401 |
Chain | Residue |
B | GLY227 |
B | GLY228 |
B | GLY229 |
B | ASP252 |
B | LEU253 |
B | VAL256 |
B | HIS274 |
B | ASN275 |
B | PHE276 |
B | HIS277 |
B | ARG291 |
B | LEU292 |
B | HOH505 |
B | HOH581 |
B | HOH584 |
B | HOH586 |
B | HOH622 |
B | HOH642 |
B | HOH666 |
B | HOH670 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue EDO B 402 |
Chain | Residue |
A | GLU90 |
A | LEU91 |
A | ARG94 |
B | ASP156 |
B | ILE157 |
B | MET343 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue EDO B 403 |
Chain | Residue |
A | ASP339 |
A | HOH536 |
A | HOH544 |
B | ARG94 |
B | ARG97 |
B | HOH569 |
B | HOH694 |
B | HOH713 |
B | HOH720 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue EDO B 404 |
Chain | Residue |
B | TRP375 |
B | HOH726 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue EDO B 405 |
Chain | Residue |
A | ASP156 |
A | ILE157 |
A | MET343 |
B | GLU90 |
B | LEU91 |
B | ARG94 |
B | HOH582 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue NA B 406 |
Chain | Residue |
B | HOH788 |
B | HOH813 |
B | PRO75 |
B | THR108 |
B | ASP110 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue ACT B 407 |
Chain | Residue |
B | ARG247 |
B | MET272 |
B | PRO281 |
B | HOH506 |
site_id | AD7 |
Number of Residues | 11 |
Details | binding site for residue B3O B 408 |
Chain | Residue |
A | MET45 |
A | LEU49 |
B | HIS133 |
B | LEU138 |
B | CYS175 |
B | ARG295 |
B | ASP296 |
B | THR338 |
B | ILE342 |
B | ALA345 |
B | LEU346 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | PHE135 | |
B | PHE135 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O04385 |
Chain | Residue | Details |
A | GLY227 | |
A | ASN275 | |
A | ARG291 | |
B | GLY227 | |
B | ASN275 | |
B | ARG291 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01020 |
Chain | Residue | Details |
A | ASP252 | |
B | ASP252 |