3APY
Properties and crystal structure of methylenetetrahydrofolate reductase from Thermus thermophilus HB8
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004489 | molecular_function | methylenetetrahydrofolate reductase [NAD(P)H] activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006555 | biological_process | L-methionine metabolic process |
| A | 0035999 | biological_process | tetrahydrofolate interconversion |
| A | 0071949 | molecular_function | FAD binding |
| A | 0106312 | molecular_function | methylenetetrahydrofolate reductase (NADH) activity |
| B | 0004489 | molecular_function | methylenetetrahydrofolate reductase [NAD(P)H] activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006555 | biological_process | L-methionine metabolic process |
| B | 0035999 | biological_process | tetrahydrofolate interconversion |
| B | 0071949 | molecular_function | FAD binding |
| B | 0106312 | molecular_function | methylenetetrahydrofolate reductase (NADH) activity |
| C | 0004489 | molecular_function | methylenetetrahydrofolate reductase [NAD(P)H] activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006555 | biological_process | L-methionine metabolic process |
| C | 0035999 | biological_process | tetrahydrofolate interconversion |
| C | 0071949 | molecular_function | FAD binding |
| C | 0106312 | molecular_function | methylenetetrahydrofolate reductase (NADH) activity |
| D | 0004489 | molecular_function | methylenetetrahydrofolate reductase [NAD(P)H] activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006555 | biological_process | L-methionine metabolic process |
| D | 0035999 | biological_process | tetrahydrofolate interconversion |
| D | 0071949 | molecular_function | FAD binding |
| D | 0106312 | molecular_function | methylenetetrahydrofolate reductase (NADH) activity |
| E | 0004489 | molecular_function | methylenetetrahydrofolate reductase [NAD(P)H] activity |
| E | 0005829 | cellular_component | cytosol |
| E | 0006555 | biological_process | L-methionine metabolic process |
| E | 0035999 | biological_process | tetrahydrofolate interconversion |
| E | 0071949 | molecular_function | FAD binding |
| E | 0106312 | molecular_function | methylenetetrahydrofolate reductase (NADH) activity |
| F | 0004489 | molecular_function | methylenetetrahydrofolate reductase [NAD(P)H] activity |
| F | 0005829 | cellular_component | cytosol |
| F | 0006555 | biological_process | L-methionine metabolic process |
| F | 0035999 | biological_process | tetrahydrofolate interconversion |
| F | 0071949 | molecular_function | FAD binding |
| F | 0106312 | molecular_function | methylenetetrahydrofolate reductase (NADH) activity |
| G | 0004489 | molecular_function | methylenetetrahydrofolate reductase [NAD(P)H] activity |
| G | 0005829 | cellular_component | cytosol |
| G | 0006555 | biological_process | L-methionine metabolic process |
| G | 0035999 | biological_process | tetrahydrofolate interconversion |
| G | 0071949 | molecular_function | FAD binding |
| G | 0106312 | molecular_function | methylenetetrahydrofolate reductase (NADH) activity |
| H | 0004489 | molecular_function | methylenetetrahydrofolate reductase [NAD(P)H] activity |
| H | 0005829 | cellular_component | cytosol |
| H | 0006555 | biological_process | L-methionine metabolic process |
| H | 0035999 | biological_process | tetrahydrofolate interconversion |
| H | 0071949 | molecular_function | FAD binding |
| H | 0106312 | molecular_function | methylenetetrahydrofolate reductase (NADH) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD A 311 |
| Chain | Residue |
| A | THR49 |
| A | ALA127 |
| A | ALA147 |
| A | TYR149 |
| A | HIS153 |
| A | SER156 |
| A | HIS165 |
| A | LYS169 |
| A | GLN180 |
| A | TYR272 |
| A | HOH322 |
| A | TYR50 |
| A | HOH342 |
| A | HOH343 |
| A | HOH447 |
| A | HOH845 |
| A | HOH860 |
| A | HIS77 |
| A | LEU104 |
| A | LEU106 |
| A | ARG107 |
| A | GLY108 |
| A | ASP109 |
| A | TYR126 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 312 |
| Chain | Residue |
| A | ARG33 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD B 311 |
| Chain | Residue |
| B | TYR50 |
| B | ALA52 |
| B | HIS77 |
| B | THR79 |
| B | LEU104 |
| B | LEU106 |
| B | ARG107 |
| B | GLY108 |
| B | ASP109 |
| B | TYR126 |
| B | ALA127 |
| B | ALA147 |
| B | TYR149 |
| B | HIS153 |
| B | SER156 |
| B | ASP162 |
| B | HIS165 |
| B | LYS169 |
| B | TYR272 |
| B | HOH315 |
| B | HOH317 |
| B | HOH331 |
| B | HOH340 |
| B | HOH814 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FAD C 311 |
| Chain | Residue |
| C | THR49 |
| C | TYR50 |
| C | HIS77 |
| C | THR79 |
| C | LEU104 |
| C | LEU106 |
| C | ARG107 |
| C | GLY108 |
| C | ASP109 |
| C | TYR126 |
| C | ALA127 |
| C | ALA147 |
| C | TYR149 |
| C | HIS153 |
| C | SER156 |
| C | HIS165 |
| C | LYS169 |
| C | TYR272 |
| C | HOH325 |
| C | HOH347 |
| C | HOH446 |
| C | HOH578 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FAD D 311 |
| Chain | Residue |
| D | THR49 |
| D | TYR50 |
| D | ALA52 |
| D | HIS77 |
| D | LEU106 |
| D | ARG107 |
| D | GLY108 |
| D | ASP109 |
| D | TYR126 |
| D | ALA127 |
| D | ALA147 |
| D | TYR149 |
| D | HIS153 |
| D | SER156 |
| D | ASP162 |
| D | HIS165 |
| D | LYS169 |
| D | GLN180 |
| D | TYR272 |
| D | HOH342 |
| D | HOH380 |
| D | HOH716 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 312 |
| Chain | Residue |
| D | ARG238 |
| D | HIS239 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FAD E 311 |
| Chain | Residue |
| E | LEU106 |
| E | ARG107 |
| E | GLY108 |
| E | ASP109 |
| E | TYR126 |
| E | ALA127 |
| E | ALA147 |
| E | TYR149 |
| E | HIS153 |
| E | SER156 |
| E | HIS165 |
| E | LYS169 |
| E | GLN180 |
| E | TYR272 |
| E | HOH328 |
| E | HOH336 |
| E | HOH341 |
| E | HOH416 |
| E | HOH732 |
| E | THR49 |
| E | TYR50 |
| E | HIS77 |
| E | LEU104 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL E 312 |
| Chain | Residue |
| G | ARG125 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FAD F 311 |
| Chain | Residue |
| F | THR49 |
| F | TYR50 |
| F | ALA52 |
| F | HIS77 |
| F | THR79 |
| F | LEU106 |
| F | ARG107 |
| F | GLY108 |
| F | ASP109 |
| F | TYR126 |
| F | ALA127 |
| F | ALA147 |
| F | TYR149 |
| F | HIS153 |
| F | SER156 |
| F | ASP162 |
| F | HIS165 |
| F | LYS169 |
| F | TYR272 |
| F | HOH533 |
| F | HOH911 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL F 312 |
| Chain | Residue |
| F | ARG238 |
| F | HIS239 |
| site_id | BC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FAD G 311 |
| Chain | Residue |
| G | THR49 |
| G | TYR50 |
| G | HIS77 |
| G | LEU104 |
| G | LEU106 |
| G | ARG107 |
| G | GLY108 |
| G | ASP109 |
| G | TYR126 |
| G | ALA127 |
| G | ALA147 |
| G | TYR149 |
| G | HIS153 |
| G | SER156 |
| G | HIS165 |
| G | LYS169 |
| G | GLN180 |
| G | TYR272 |
| G | HOH320 |
| G | HOH340 |
| G | HOH342 |
| G | HOH668 |
| G | HOH678 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL G 312 |
| Chain | Residue |
| G | ARG33 |
| site_id | BC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD H 311 |
| Chain | Residue |
| H | THR49 |
| H | TYR50 |
| H | ALA52 |
| H | HIS77 |
| H | LEU104 |
| H | LEU106 |
| H | ARG107 |
| H | GLY108 |
| H | ASP109 |
| H | TYR126 |
| H | ALA127 |
| H | ALA147 |
| H | TYR149 |
| H | HIS153 |
| H | SER156 |
| H | ASP162 |
| H | HIS165 |
| H | LYS169 |
| H | TYR272 |
| H | HOH325 |
| H | HOH331 |
| H | HOH333 |
| H | HOH344 |
| H | HOH452 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL H 312 |
| Chain | Residue |
| H | ARG238 |
| H | HIS239 |
