1P0Y
Crystal structure of the SET domain of LSMT bound to MeLysine and AdoHcy
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009507 | cellular_component | chloroplast |
A | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
A | 0018022 | biological_process | peptidyl-lysine methylation |
A | 0030785 | molecular_function | [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity |
B | 0009507 | cellular_component | chloroplast |
B | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
B | 0018022 | biological_process | peptidyl-lysine methylation |
B | 0030785 | molecular_function | [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity |
C | 0009507 | cellular_component | chloroplast |
C | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
C | 0018022 | biological_process | peptidyl-lysine methylation |
C | 0030785 | molecular_function | [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE SAH A 800 |
Chain | Residue |
A | GLU80 |
A | TYR300 |
A | GLY301 |
A | PHE302 |
A | HOH803 |
A | HOH825 |
A | HOH858 |
A | HOH867 |
A | HOH982 |
A | HOH997 |
C | MLZ900 |
A | GLY81 |
A | LEU82 |
A | SER221 |
A | ARG222 |
A | ASP239 |
A | ASN242 |
A | HIS243 |
A | TYR287 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE SAH B 801 |
Chain | Residue |
B | GLU80 |
B | LEU82 |
B | SER221 |
B | ARG222 |
B | ASP239 |
B | LEU240 |
B | ILE241 |
B | ASN242 |
B | HIS243 |
B | TYR287 |
B | TYR300 |
B | GLY301 |
B | PHE302 |
B | HOH802 |
B | HOH804 |
B | HOH811 |
B | HOH908 |
B | HOH909 |
C | PHE263 |
C | HOH935 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE SAH C 802 |
Chain | Residue |
C | GLU80 |
C | LEU82 |
C | SER221 |
C | ARG222 |
C | ASP239 |
C | LEU240 |
C | ASN242 |
C | HIS243 |
C | TYR287 |
C | TYR300 |
C | GLY301 |
C | PHE302 |
C | MLZ902 |
C | HOH904 |
C | HOH909 |
C | HOH954 |
C | HOH1097 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MLZ C 900 |
Chain | Residue |
A | ARG222 |
A | PHE224 |
A | SER225 |
A | ARG226 |
A | ASP239 |
A | TYR254 |
A | TYR287 |
A | TYR300 |
A | SAH800 |
A | HOH990 |
C | HOH996 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MLZ C 901 |
Chain | Residue |
B | ARG222 |
B | PHE224 |
B | SER225 |
B | ARG226 |
B | ASP239 |
B | ILE241 |
B | HIS252 |
B | TYR287 |
C | HOH906 |
C | HOH916 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE MLZ C 902 |
Chain | Residue |
C | SER221 |
C | ARG222 |
C | ALA223 |
C | PHE224 |
C | SER225 |
C | ARG226 |
C | ASP239 |
C | ILE241 |
C | TYR254 |
C | TYR287 |
C | LYS291 |
C | TYR300 |
C | SAH802 |
C | HOH1062 |
C | HOH1067 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU80 | |
A | ASN242 | |
B | GLU80 | |
B | ASN242 | |
C | GLU80 | |
C | ASN242 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12819771, ECO:0000269|PubMed:16682405 |
Chain | Residue | Details |
A | ARG222 | |
B | TYR254 | |
B | TYR287 | |
B | TYR300 | |
C | ARG222 | |
C | ARG226 | |
C | ASP239 | |
C | TYR254 | |
C | TYR287 | |
C | TYR300 | |
A | ARG226 | |
A | ASP239 | |
A | TYR254 | |
A | TYR287 | |
A | TYR300 | |
B | ARG222 | |
B | ARG226 | |
B | ASP239 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1mlv |
Chain | Residue | Details |
A | TYR287 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1mlv |
Chain | Residue | Details |
B | TYR287 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1mlv |
Chain | Residue | Details |
C | TYR287 |
site_id | MCSA1 |
Number of Residues | 1 |
Details | M-CSA 604 |
Chain | Residue | Details |
A | TYR287 | activator, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 1 |
Details | M-CSA 604 |
Chain | Residue | Details |
B | TYR287 | activator, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 1 |
Details | M-CSA 604 |
Chain | Residue | Details |
C | TYR287 | activator, proton acceptor, proton donor |