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The crystal structure of isomerase domain of glucosamine-6-phosphate synthase from Candida albicans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0097367 | molecular_function | carbohydrate derivative binding |
| A | 1901135 | biological_process | carbohydrate derivative metabolic process |
| B | 0097367 | molecular_function | carbohydrate derivative binding |
| B | 1901135 | biological_process | carbohydrate derivative metabolic process |
| C | 0097367 | molecular_function | carbohydrate derivative binding |
| C | 1901135 | biological_process | carbohydrate derivative metabolic process |
| D | 0097367 | molecular_function | carbohydrate derivative binding |
| D | 1901135 | biological_process | carbohydrate derivative metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 713 |
| Chain | Residue |
| A | LYS590 |
| A | HOH5163 |
| A | HOH5703 |
| B | VAL600 |
| B | LEU605 |
| B | GLY608 |
| B | ILE609 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 5001 |
| Chain | Residue |
| A | THR487 |
| A | UD15002 |
| A | HOH5011 |
| A | HOH5012 |
| A | SER484 |
| A | ARG485 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 5002 |
| Chain | Residue |
| B | SER484 |
| B | ARG485 |
| B | THR487 |
| B | UD15003 |
| B | HOH5008 |
| B | HOH5009 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT C 713 |
| Chain | Residue |
| C | LEU605 |
| C | GLY608 |
| C | ILE609 |
| C | HOH5478 |
| C | HOH5481 |
| D | LYS590 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 5003 |
| Chain | Residue |
| C | SER484 |
| C | ARG485 |
| C | THR487 |
| C | UD15004 |
| C | HOH5010 |
| C | HOH5752 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 5004 |
| Chain | Residue |
| D | SER484 |
| D | ARG485 |
| D | THR487 |
| D | UD15005 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UD1 A 5002 |
| Chain | Residue |
| A | ARG372 |
| A | GLY383 |
| A | GLY384 |
| A | GLY474 |
| A | VAL476 |
| A | SER484 |
| A | THR487 |
| A | CYS489 |
| A | GLY490 |
| A | VAL491 |
| A | HIS492 |
| A | NA5001 |
| A | HOH5143 |
| A | HOH5144 |
| A | HOH5250 |
| A | HOH5662 |
| A | HOH5663 |
| A | HOH5698 |
| A | HOH5723 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE F6R A 5003 |
| Chain | Residue |
| A | CYS403 |
| A | GLY404 |
| A | THR405 |
| A | SER406 |
| A | SER450 |
| A | GLN451 |
| A | SER452 |
| A | THR455 |
| A | ALA502 |
| A | SER503 |
| A | LYS588 |
| A | GLU591 |
| A | HOH5036 |
| A | HOH5037 |
| A | HOH5198 |
| A | HOH5245 |
| A | HOH5630 |
| site_id | AC9 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE UD1 B 5003 |
| Chain | Residue |
| B | ARG372 |
| B | GLY383 |
| B | GLY384 |
| B | GLY474 |
| B | VAL476 |
| B | VAL479 |
| B | SER484 |
| B | THR487 |
| B | CYS489 |
| B | GLY490 |
| B | VAL491 |
| B | HIS492 |
| B | NA5002 |
| B | HOH5021 |
| B | HOH5022 |
| B | HOH5336 |
| B | HOH5337 |
| B | HOH5350 |
| site_id | BC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE F6R B 5004 |
| Chain | Residue |
| B | LYS588 |
| B | GLU591 |
| B | HOH5157 |
| B | HOH5158 |
| B | HOH5345 |
| B | HOH5618 |
| B | HOH5702 |
| B | CYS403 |
| B | GLY404 |
| B | THR405 |
| B | SER406 |
| B | SER450 |
| B | GLN451 |
| B | SER452 |
| B | THR455 |
| B | ALA502 |
| B | SER503 |
| site_id | BC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE UD1 C 5004 |
| Chain | Residue |
| C | ARG372 |
| C | GLY383 |
| C | GLY384 |
| C | GLY474 |
| C | VAL476 |
| C | SER484 |
| C | THR487 |
| C | CYS489 |
| C | GLY490 |
| C | VAL491 |
| C | HIS492 |
| C | NA5003 |
| C | HOH5018 |
| C | HOH5186 |
| C | HOH5281 |
| C | HOH5282 |
| C | HOH5283 |
| C | HOH5408 |
| C | HOH5423 |
| C | HOH5428 |
| C | HOH5429 |
| site_id | BC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE F6R C 5005 |
| Chain | Residue |
| C | CYS403 |
| C | THR405 |
| C | SER406 |
| C | SER450 |
| C | GLN451 |
| C | SER452 |
| C | THR455 |
| C | ALA502 |
| C | SER503 |
| C | LYS588 |
| C | GLU591 |
| C | HOH5111 |
| C | HOH5204 |
| C | HOH5388 |
| C | HOH5673 |
| site_id | BC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE UD1 D 5005 |
| Chain | Residue |
| D | ARG372 |
| D | GLY383 |
| D | GLY384 |
| D | GLY474 |
| D | VAL476 |
| D | SER484 |
| D | THR487 |
| D | CYS489 |
| D | GLY490 |
| D | VAL491 |
| D | HIS492 |
| D | NA5004 |
| D | HOH5011 |
| D | HOH5013 |
| D | HOH5014 |
| D | HOH5047 |
| D | HOH5125 |
| D | HOH5157 |
| site_id | BC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE F6R D 5006 |
| Chain | Residue |
| D | CYS403 |
| D | GLY404 |
| D | THR405 |
| D | SER406 |
| D | SER450 |
| D | GLN451 |
| D | SER452 |
| D | THR455 |
| D | ALA502 |
| D | SER503 |
| D | LYS588 |
| D | GLU591 |
| D | HOH5021 |
| D | HOH5023 |
| D | HOH5105 |
| D | HOH5156 |
| D | HOH5174 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1jxa |
| Chain | Residue | Details |
| B | LYS588 | |
| B | GLU591 | |
| B | GLU584 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1jxa |
| Chain | Residue | Details |
| C | LYS588 | |
| C | GLU591 | |
| C | GLU584 |
| site_id | CSA3 |
| Number of Residues | 8 |
| Details | Annotated By Reference To The Literature 1jxa |
| Chain | Residue | Details |
| A | LYS588 | |
| A | GLU591 | |
| A | GLU584 | |
| C | HIS607 | |
| D | LYS588 | |
| D | GLU591 | |
| D | GLU584 | |
| B | HIS607 |
