6IX9
The structure of LepI C52A in complex with SAM and leporin C
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008171 | molecular_function | O-methyltransferase 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 | obsolete organic cyclic compound biosynthetic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008171 | molecular_function | O-methyltransferase 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 | obsolete organic cyclic compound biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue SAM A 401 |
| Chain | Residue |
| A | GLY227 |
| A | LEU292 |
| A | HOH588 |
| A | HOH589 |
| A | HOH610 |
| A | HOH648 |
| A | HOH681 |
| A | HOH691 |
| A | HOH700 |
| A | GLY229 |
| A | ASP252 |
| A | LEU253 |
| A | VAL256 |
| A | HIS274 |
| A | ASN275 |
| A | PHE276 |
| A | ARG291 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 402 |
| Chain | Residue |
| A | THR336 |
| A | ASP339 |
| B | ARG94 |
| B | HOH512 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue B0O B 401 |
| Chain | Residue |
| A | MET45 |
| A | SER48 |
| B | HIS133 |
| B | CYS175 |
| B | PHE189 |
| B | LEU192 |
| B | ARG295 |
| B | ASP296 |
| B | ILE342 |
| B | LEU346 |
| B | HOH513 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | binding site for residue SAM B 402 |
| Chain | Residue |
| B | LEU193 |
| 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 | HOH550 |
| B | HOH585 |
| B | HOH602 |
| B | HOH630 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | SER115 |
| B | SER116 |
| B | ASN117 |
| B | GLN120 |
| B | HOH509 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 404 |
| Chain | Residue |
| B | ASN379 |
| B | HOH518 |
| B | HOH654 |
| B | HOH710 |
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 |
