1NBU
7,8-Dihydroneopterin Aldolase Complexed with Product From Mycobacterium Tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| A | 0006760 | biological_process | folic acid-containing compound metabolic process |
| B | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| B | 0006760 | biological_process | folic acid-containing compound metabolic process |
| C | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| C | 0006760 | biological_process | folic acid-containing compound metabolic process |
| D | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| D | 0006760 | biological_process | folic acid-containing compound metabolic process |
| E | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| E | 0006760 | biological_process | folic acid-containing compound metabolic process |
| F | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| F | 0006760 | biological_process | folic acid-containing compound metabolic process |
| G | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| G | 0006760 | biological_process | folic acid-containing compound metabolic process |
| H | 0004150 | molecular_function | dihydroneopterin aldolase activity |
| H | 0006760 | biological_process | folic acid-containing compound metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PH2 C 120 |
| Chain | Residue |
| A | THR51 |
| C | ILE73 |
| C | GLU74 |
| C | LYS99 |
| C | HOH9166 |
| A | TYR52 |
| A | ASP53 |
| A | TYR54 |
| A | VAL55 |
| C | GLY17 |
| C | VAL18 |
| C | GLU22 |
| C | LEU72 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PH2 D 220 |
| Chain | Residue |
| B | LEU48 |
| B | THR51 |
| B | TYR52 |
| B | ASP53 |
| B | TYR54 |
| B | VAL55 |
| D | GLY17 |
| D | VAL18 |
| D | GLU22 |
| D | LEU72 |
| D | ILE73 |
| D | GLU74 |
| D | LYS99 |
| D | HOH9116 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PH2 B 320 |
| Chain | Residue |
| B | GLY17 |
| B | VAL18 |
| B | GLU22 |
| B | LEU72 |
| B | ILE73 |
| B | GLU74 |
| B | LYS99 |
| B | HOH9023 |
| C | THR51 |
| C | TYR52 |
| C | ASP53 |
| C | TYR54 |
| C | VAL55 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PH2 A 420 |
| Chain | Residue |
| A | GLY17 |
| A | VAL18 |
| A | GLU22 |
| A | LEU72 |
| A | ILE73 |
| A | GLU74 |
| A | LYS99 |
| A | HOH9140 |
| D | LEU48 |
| D | THR51 |
| D | TYR52 |
| D | ASP53 |
| D | TYR54 |
| D | VAL55 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PH2 G 520 |
| Chain | Residue |
| E | LEU48 |
| E | THR51 |
| E | TYR52 |
| E | ASP53 |
| E | TYR54 |
| E | VAL55 |
| G | GLY17 |
| G | VAL18 |
| G | GLU22 |
| G | LEU72 |
| G | ILE73 |
| G | GLU74 |
| G | LYS99 |
| G | HOH9047 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PH2 H 620 |
| Chain | Residue |
| F | LEU48 |
| F | THR51 |
| F | TYR52 |
| F | ASP53 |
| F | TYR54 |
| F | VAL55 |
| F | HOH9340 |
| H | GLY17 |
| H | VAL18 |
| H | GLU22 |
| H | LEU72 |
| H | ILE73 |
| H | GLU74 |
| H | LYS99 |
| H | HOH9005 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PH2 F 720 |
| Chain | Residue |
| F | GLY17 |
| F | VAL18 |
| F | GLU22 |
| F | LEU72 |
| F | ILE73 |
| F | GLU74 |
| F | LYS99 |
| F | HOH9017 |
| G | LEU48 |
| G | THR51 |
| G | TYR52 |
| G | ASP53 |
| G | TYR54 |
| G | VAL55 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PH2 E 820 |
| Chain | Residue |
| E | GLU22 |
| E | LEU72 |
| E | ILE73 |
| E | GLU74 |
| E | LYS99 |
| E | HOH9003 |
| H | LEU48 |
| H | THR51 |
| H | TYR52 |
| H | ASP53 |
| H | TYR54 |
| H | VAL55 |
| E | GLY17 |
| E | VAL18 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P56740, ECO:0000305 |
| Chain | Residue | Details |
| C | LYS99 | |
| D | LYS99 | |
| F | LYS99 | |
| G | LYS99 | |
| H | LYS99 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:15876368, ECO:0007744|PDB:1NBU |
| Chain | Residue | Details |
| C | GLU22 | |
| G | GLU22 | |
| G | TYR54 | |
| G | ILE73 | |
| H | GLU22 | |
| H | TYR54 | |
| H | ILE73 | |
| C | TYR54 | |
| C | ILE73 | |
| D | GLU22 | |
| D | TYR54 | |
| D | ILE73 | |
| F | GLU22 | |
| F | TYR54 | |
| F | ILE73 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dhn |
| Chain | Residue | Details |
| A | GLU22 | |
| A | LYS99 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dhn |
| Chain | Residue | Details |
| E | GLU22 | |
| E | LYS99 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dhn |
| Chain | Residue | Details |
| F | GLU22 | |
| F | LYS99 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dhn |
| Chain | Residue | Details |
| G | GLU22 | |
| G | LYS99 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dhn |
| Chain | Residue | Details |
| H | GLU22 | |
| H | LYS99 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dhn |
| Chain | Residue | Details |
| B | GLU22 | |
| B | LYS99 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dhn |
| Chain | Residue | Details |
| D | GLU22 | |
| D | LYS99 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dhn |
| Chain | Residue | Details |
| C | GLU22 | |
| C | LYS99 |
