2H2E
Structure of Rubisco LSMT bound to AzaAdoMet and Lysine
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 | 17 |
| Details | BINDING SITE FOR RESIDUE SA8 A 800 |
| Chain | Residue |
| A | GLU80 |
| A | TYR287 |
| A | PHE302 |
| A | LYS902 |
| A | HOH903 |
| A | HOH939 |
| A | HOH951 |
| A | HOH975 |
| A | HOH987 |
| A | GLY81 |
| A | LEU82 |
| A | SER221 |
| A | ARG222 |
| A | ASP239 |
| A | LEU240 |
| A | ASN242 |
| A | HIS243 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SA8 B 801 |
| Chain | Residue |
| B | LEU82 |
| B | SER221 |
| B | ARG222 |
| B | ASP239 |
| B | LEU240 |
| B | ASN242 |
| B | HIS243 |
| B | TYR287 |
| B | PHE302 |
| B | LYS900 |
| B | HOH901 |
| B | HOH904 |
| B | HOH913 |
| B | HOH929 |
| B | HOH948 |
| B | HOH958 |
| B | HOH981 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SA8 C 802 |
| Chain | Residue |
| C | GLY81 |
| C | LEU82 |
| C | SER221 |
| C | ARG222 |
| C | ASP239 |
| C | LEU240 |
| C | ASN242 |
| C | HIS243 |
| C | TYR287 |
| C | LYS901 |
| C | HOH924 |
| C | HOH983 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LYS B 900 |
| Chain | Residue |
| B | SER221 |
| B | ARG222 |
| B | ALA223 |
| B | PHE224 |
| B | SER225 |
| B | ASP239 |
| B | TYR287 |
| B | TYR300 |
| B | SA8801 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LYS C 901 |
| Chain | Residue |
| C | ARG222 |
| C | SER225 |
| C | ARG226 |
| C | ASP239 |
| C | TYR254 |
| C | TYR287 |
| C | TYR300 |
| C | SA8802 |
| C | HOH948 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LYS A 902 |
| Chain | Residue |
| A | SER221 |
| A | ARG222 |
| A | ALA223 |
| A | PHE224 |
| A | TYR287 |
| A | TYR300 |
| A | SA8800 |
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 |
| C | ARG222 | |
| C | ARG226 | |
| C | ASP239 | |
| C | TYR254 | |
| C | TYR287 | |
| C | TYR300 | |
| A | ARG222 | |
| A | ARG226 | |
| A | ASP239 | |
| A | TYR254 | |
| A | TYR287 | |
| A | TYR300 | |
| B | ARG222 | |
| B | ARG226 | |
| B | ASP239 | |
| B | TYR254 | |
| B | TYR287 | |
| B | TYR300 |
Catalytic Information from CSA
| 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 |
