6DC1
Directed evolutionary changes in Kemp Eliminase KE07 - Crystal 25 round 7
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000105 | biological_process | L-histidine biosynthetic process |
| A | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| B | 0000105 | biological_process | L-histidine biosynthetic process |
| B | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| C | 0000105 | biological_process | L-histidine biosynthetic process |
| C | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| D | 0000105 | biological_process | L-histidine biosynthetic process |
| D | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| E | 0000105 | biological_process | L-histidine biosynthetic process |
| E | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| F | 0000105 | biological_process | L-histidine biosynthetic process |
| F | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| G | 0000105 | biological_process | L-histidine biosynthetic process |
| G | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| H | 0000105 | biological_process | L-histidine biosynthetic process |
| H | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| I | 0000105 | biological_process | L-histidine biosynthetic process |
| I | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| J | 0000105 | biological_process | L-histidine biosynthetic process |
| J | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| K | 0000105 | biological_process | L-histidine biosynthetic process |
| K | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
| L | 0000105 | biological_process | L-histidine biosynthetic process |
| L | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue 6VP A 301 |
| Chain | Residue |
| A | ALA9 |
| A | TRP50 |
| A | GLU101 |
| A | TYR128 |
| A | ARG202 |
| A | LYS222 |
| A | HOH435 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue B3P A 302 |
| Chain | Residue |
| A | GLY121 |
| A | SER122 |
| A | GLU161 |
| A | HOH427 |
| D | ALA117 |
| D | SER122 |
| D | GLU161 |
| D | HOH317 |
| D | HOH353 |
| A | ALA117 |
| A | GLN118 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue 6VP B 301 |
| Chain | Residue |
| B | ALA9 |
| B | ILE11 |
| B | TRP50 |
| B | GLU101 |
| B | TYR128 |
| B | ARG202 |
| B | LYS222 |
| B | HOH445 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue B3P C 301 |
| Chain | Residue |
| B | ALA117 |
| B | GLY121 |
| B | SER122 |
| B | GLU161 |
| C | ALA117 |
| C | GLY121 |
| C | SER122 |
| C | GLU161 |
| C | HOH431 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue PEG C 302 |
| Chain | Residue |
| C | ALA9 |
| C | TRP50 |
| C | GLU101 |
| C | TYR128 |
| C | ARG202 |
| C | LYS222 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue PEG G 301 |
| Chain | Residue |
| G | TRP50 |
| G | TYR128 |
| G | ARG202 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue 6VP H 301 |
| Chain | Residue |
| H | ALA9 |
| H | ILE11 |
| H | TRP50 |
| H | GLU101 |
| H | TYR128 |
| H | HIS201 |
| H | ARG202 |
| H | LYS222 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue 6VP K 301 |
| Chain | Residue |
| K | ALA9 |
| K | ILE11 |
| K | TRP50 |
| K | GLU101 |
| K | TYR128 |
| K | LYS222 |
| K | HOH441 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue TRS L 301 |
| Chain | Residue |
| L | ILE11 |
| L | TRP50 |
| L | TYR128 |
| L | ARG202 |
| L | LYS222 |
