4RC1
Structure of the methanofuran/methanopterin biosynthetic enzyme MJ1099 from Methanocaldococcus jannaschii with PRPP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 2001120 | biological_process | methanofuran biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 2001120 | biological_process | methanofuran biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016830 | molecular_function | carbon-carbon lyase activity |
| C | 2001120 | biological_process | methanofuran biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016830 | molecular_function | carbon-carbon lyase activity |
| D | 2001120 | biological_process | methanofuran biosynthetic process |
| E | 0016829 | molecular_function | lyase activity |
| E | 0016830 | molecular_function | carbon-carbon lyase activity |
| E | 2001120 | biological_process | methanofuran biosynthetic process |
| F | 0016829 | molecular_function | lyase activity |
| F | 0016830 | molecular_function | carbon-carbon lyase activity |
| F | 2001120 | biological_process | methanofuran biosynthetic process |
| G | 0016829 | molecular_function | lyase activity |
| G | 0016830 | molecular_function | carbon-carbon lyase activity |
| G | 2001120 | biological_process | methanofuran biosynthetic process |
| H | 0016829 | molecular_function | lyase activity |
| H | 0016830 | molecular_function | carbon-carbon lyase activity |
| H | 2001120 | biological_process | methanofuran biosynthetic process |
| I | 0016829 | molecular_function | lyase activity |
| I | 0016830 | molecular_function | carbon-carbon lyase activity |
| I | 2001120 | biological_process | methanofuran biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 301 |
| Chain | Residue |
| B | LYS27 |
| B | LYS155 |
| B | SER188 |
| B | ARG208 |
| B | GLY209 |
| B | ARG217 |
| B | HOH402 |
| B | HOH403 |
| B | HOH410 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 C 301 |
| Chain | Residue |
| C | LYS27 |
| C | LYS155 |
| C | GLY187 |
| C | SER188 |
| C | VAL207 |
| C | ARG208 |
| C | GLY209 |
| C | ARG217 |
| C | HOH416 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 D 301 |
| Chain | Residue |
| D | LYS27 |
| D | LYS155 |
| D | SER188 |
| D | ARG208 |
| D | GLY209 |
| D | ARG217 |
| D | HOH402 |
| D | HOH416 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 E 301 |
| Chain | Residue |
| E | LYS27 |
| E | LYS155 |
| E | SER188 |
| E | ARG208 |
| E | GLY209 |
| E | HOH413 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 F 301 |
| Chain | Residue |
| F | LYS27 |
| F | LYS155 |
| F | GLY187 |
| F | SER188 |
| F | ARG208 |
| F | GLY209 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 I 301 |
| Chain | Residue |
| I | LYS27 |
| I | LYS155 |
| I | GLY187 |
| I | SER188 |
| I | ARG208 |
| I | GLY209 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | ACT_SITE: Schiff-base intermediate with substrate => ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000305|PubMed:25905665 |
| Chain | Residue | Details |
| A | LYS27 | |
| B | LYS27 | |
| C | LYS27 | |
| D | LYS27 | |
| E | LYS27 | |
| F | LYS27 | |
| G | LYS27 | |
| H | LYS27 | |
| I | LYS27 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000305|PubMed:25905665 |
| Chain | Residue | Details |
| A | LYS85 | |
| B | LYS85 | |
| C | LYS85 | |
| D | LYS85 | |
| E | LYS85 | |
| F | LYS85 | |
| G | LYS85 | |
| H | LYS85 | |
| I | LYS85 |
