4LRT
Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003852 | molecular_function | 2-isopropylmalate synthase activity |
| A | 0008701 | molecular_function | 4-hydroxy-2-oxovalerate aldolase activity |
| A | 0009056 | biological_process | catabolic process |
| A | 0009098 | biological_process | L-leucine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016833 | molecular_function | oxo-acid-lyase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008774 | molecular_function | acetaldehyde dehydrogenase (acetylating) activity |
| B | 0009056 | biological_process | catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0051287 | molecular_function | NAD binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003852 | molecular_function | 2-isopropylmalate synthase activity |
| C | 0008701 | molecular_function | 4-hydroxy-2-oxovalerate aldolase activity |
| C | 0009056 | biological_process | catabolic process |
| C | 0009098 | biological_process | L-leucine biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016833 | molecular_function | oxo-acid-lyase activity |
| C | 0030145 | molecular_function | manganese ion binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008774 | molecular_function | acetaldehyde dehydrogenase (acetylating) activity |
| D | 0009056 | biological_process | catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PYR A 401 |
| Chain | Residue |
| A | ARG21 |
| A | HOH543 |
| A | ASP22 |
| A | MET145 |
| A | VAL173 |
| A | SER175 |
| A | HIS204 |
| A | HIS206 |
| A | TYR295 |
| A | MG403 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 402 |
| Chain | Residue |
| A | VAL180 |
| A | SER182 |
| C | GLN221 |
| C | HOH622 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 403 |
| Chain | Residue |
| A | ASP22 |
| A | HIS204 |
| A | HIS206 |
| A | PYR401 |
| A | HOH543 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 401 |
| Chain | Residue |
| B | ARG268 |
| B | ASP269 |
| B | ILE270 |
| B | HOH673 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 402 |
| Chain | Residue |
| B | LYS98 |
| C | GLU135 |
| C | HOH693 |
| C | HOH723 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA B 403 |
| Chain | Residue |
| B | CYS146 |
| B | ASN296 |
| B | HOH790 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 404 |
| Chain | Residue |
| B | ALA108 |
| B | PRO139 |
| B | HOH629 |
| B | HOH798 |
| site_id | AC8 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE COA B 405 |
| Chain | Residue |
| B | GLY30 |
| B | PRO31 |
| B | GLY32 |
| B | ASN33 |
| B | ILE34 |
| B | GLY55 |
| B | VAL56 |
| B | SER60 |
| B | ALA94 |
| B | THR95 |
| B | ALA99 |
| B | PRO119 |
| B | CYS146 |
| B | THR182 |
| B | ASN296 |
| B | LEU297 |
| B | HOH501 |
| B | HOH502 |
| B | HOH506 |
| B | HOH511 |
| B | HOH522 |
| B | HOH533 |
| B | HOH543 |
| B | HOH554 |
| B | HOH556 |
| B | HOH573 |
| B | HOH608 |
| B | HOH702 |
| B | HOH717 |
| B | HOH728 |
| B | HOH780 |
| B | HOH781 |
| B | HOH801 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PYR C 401 |
| Chain | Residue |
| C | ARG21 |
| C | ASP22 |
| C | PHE143 |
| C | MET145 |
| C | VAL173 |
| C | SER175 |
| C | HIS204 |
| C | HIS206 |
| C | TYR295 |
| C | MG404 |
| C | HOH567 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 402 |
| Chain | Residue |
| C | ILE161 |
| C | ASP164 |
| C | HOH690 |
| C | HOH739 |
| C | HOH849 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 403 |
| Chain | Residue |
| A | HOH663 |
| A | HOH699 |
| C | PRO312 |
| C | ALA313 |
| C | HIS314 |
| C | HOH608 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 404 |
| Chain | Residue |
| C | ASP22 |
| C | HIS204 |
| C | HIS206 |
| C | PYR401 |
| C | HOH567 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 401 |
| Chain | Residue |
| D | HOH797 |
| A | ASP183 |
| A | ARG187 |
| D | ARG251 |
| D | HOH632 |
| D | HOH743 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA D 402 |
| Chain | Residue |
| D | CYS146 |
| D | ASN296 |
| D | HOH819 |
| site_id | BC6 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE COA D 403 |
| Chain | Residue |
| D | GLY30 |
| D | PRO31 |
| D | GLY32 |
| D | ASN33 |
| D | ILE34 |
| D | GLY55 |
| D | VAL56 |
| D | SER60 |
| D | ALA94 |
| D | THR95 |
| D | ALA99 |
| D | PRO119 |
| D | CYS146 |
| D | THR182 |
| D | ASN296 |
| D | LEU297 |
| D | HOH503 |
| D | HOH519 |
| D | HOH531 |
| D | HOH563 |
| D | HOH566 |
| D | HOH574 |
| D | HOH585 |
| D | HOH598 |
| D | HOH616 |
| D | HOH630 |
| D | HOH677 |
| D | HOH785 |
| D | HOH792 |
| D | HOH795 |
| D | HOH820 |
