2HNK
Crystal structure of SAM-dependent O-methyltransferase from pathogenic bacterium Leptospira interrogans
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008171 | molecular_function | O-methyltransferase activity |
A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
A | 0032259 | biological_process | methylation |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0008171 | molecular_function | O-methyltransferase activity |
B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
B | 0032259 | biological_process | methylation |
C | 0008168 | molecular_function | methyltransferase activity |
C | 0008171 | molecular_function | O-methyltransferase activity |
C | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
C | 0032259 | biological_process | methylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A1001 |
Chain | Residue |
A | ARG229 |
A | ARG231 |
A | LEU232 |
A | HIS234 |
A | HOH3133 |
C | LYS57 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B1002 |
Chain | Residue |
B | LEU232 |
B | LYS57 |
B | ARG229 |
B | ARG231 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C1003 |
Chain | Residue |
A | LYS57 |
C | ARG229 |
C | ARG231 |
C | LEU232 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C1004 |
Chain | Residue |
A | ARG22 |
C | TYR209 |
C | ASN210 |
C | HOH3124 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE SAH A2001 |
Chain | Residue |
A | MET42 |
A | GLN43 |
A | GLY68 |
A | THR69 |
A | PHE70 |
A | SER74 |
A | ASP92 |
A | VAL93 |
A | ALA121 |
A | ASP154 |
A | ASP156 |
A | TYR163 |
A | HOH3106 |
A | HOH3116 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE SAH B2002 |
Chain | Residue |
B | MET42 |
B | GLN43 |
B | GLY68 |
B | THR69 |
B | PHE70 |
B | SER74 |
B | CYS91 |
B | ASP92 |
B | VAL93 |
B | ALA121 |
B | PHE152 |
B | ASP154 |
B | ASP156 |
B | TYR163 |
B | HOH3041 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE SAH C2003 |
Chain | Residue |
C | MET42 |
C | GLN43 |
C | GLY68 |
C | THR69 |
C | PHE70 |
C | SER74 |
C | ASP92 |
C | VAL93 |
C | TRP97 |
C | ALA121 |
C | ASP154 |
C | ASP156 |
C | TYR163 |
C | HOH3017 |
C | HOH3114 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG A3001 |
Chain | Residue |
A | GLY60 |
A | ASP149 |
A | LYS172 |
A | PEG3003 |
A | HOH3148 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG C3002 |
Chain | Residue |
A | PEG3003 |
C | GLY60 |
C | LYS172 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PEG A3003 |
Chain | Residue |
A | ILE58 |
A | SER59 |
A | PEG3001 |
C | ILE58 |
C | SER59 |
C | GLY60 |
C | PEG3002 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG A3004 |
Chain | Residue |
A | TRP184 |
A | ASP185 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG C3005 |
Chain | Residue |
C | TRP184 |
C | GLU195 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG B3006 |
Chain | Residue |
B | LEU122 |
B | ASN162 |
B | HOH3093 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG A3007 |
Chain | Residue |
A | LYS106 |
A | GLU107 |
A | HOH3165 |