4JBE
1.95 Angstrom Crystal Structure of Gamma-glutamyl phosphate Reductase from Saccharomonospora viridis.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004350 | molecular_function | glutamate-5-semialdehyde dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0055129 | biological_process | L-proline biosynthetic process |
| B | 0004350 | molecular_function | glutamate-5-semialdehyde dehydrogenase activity |
| 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 | 0046872 | molecular_function | metal ion binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0055129 | biological_process | L-proline biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 501 |
| Chain | Residue |
| A | SER209 |
| A | SER212 |
| A | HOH663 |
| A | HOH837 |
| A | HOH867 |
| A | HOH868 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 502 |
| Chain | Residue |
| A | HOH679 |
| A | HOH776 |
| A | ALA273 |
| A | GLU277 |
| A | HOH627 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 503 |
| Chain | Residue |
| A | GLU219 |
| A | HOH924 |
| A | HOH925 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 504 |
| Chain | Residue |
| A | HOH827 |
| A | HOH830 |
| A | HOH851 |
| A | HOH899 |
| A | HOH900 |
| A | HOH939 |
| A | HOH961 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 505 |
| Chain | Residue |
| A | GLY25 |
| A | HOH713 |
| A | HOH744 |
| A | HOH946 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 506 |
| Chain | Residue |
| A | HOH721 |
| A | HOH780 |
| A | HOH952 |
| A | HOH953 |
| A | HOH954 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 507 |
| Chain | Residue |
| A | ARG149 |
| A | SER152 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 508 |
| Chain | Residue |
| A | LEU197 |
| A | PRO198 |
| A | ASP199 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 509 |
| Chain | Residue |
| A | PRO27 |
| A | ASP28 |
| A | ARG98 |
| A | HOH661 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 510 |
| Chain | Residue |
| A | ASN124 |
| A | GLY208 |
| A | THR213 |
| A | HOH622 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 512 |
| Chain | Residue |
| A | ARG160 |
| A | ARG329 |
| A | HOH616 |
| A | HOH696 |
| A | HOH844 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 513 |
| Chain | Residue |
| A | ASN263 |
| A | ARG369 |
| A | ASP372 |
| A | LYS375 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 514 |
| Chain | Residue |
| A | ARG369 |
| A | HOH792 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME A 515 |
| Chain | Residue |
| A | VAL261 |
| A | CYS262 |
| A | ASN263 |
| A | HOH792 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 516 |
| Chain | Residue |
| A | TYR125 |
| A | GLU126 |
| A | ARG128 |
| A | ARG207 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES A 517 |
| Chain | Residue |
| A | ALA44 |
| A | HIS45 |
| A | ASP47 |
| A | ALA48 |
| A | ALA325 |
| A | GLU352 |
| A | HOH616 |
| A | HOH794 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 501 |
| Chain | Residue |
| B | ASP244 |
| B | ASP244 |
| B | ASP246 |
| B | ASP246 |
| B | HOH726 |
| B | HOH726 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 502 |
| Chain | Residue |
| B | ALA273 |
| B | GLU277 |
| B | HOH743 |
| B | HOH768 |
| B | HOH769 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA B 503 |
| Chain | Residue |
| B | HOH774 |
| B | HOH813 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 504 |
| Chain | Residue |
| B | GLU284 |
| B | GLU288 |
| B | HOH772 |
| B | HOH773 |
| B | HOH812 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 505 |
| Chain | Residue |
| B | ASN124 |
| B | GLY208 |
| B | THR213 |
| B | HOH677 |
| B | HOH818 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 506 |
| Chain | Residue |
| B | ASN263 |
| B | ARG369 |
| B | ASP372 |
| B | LYS375 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 508 |
| Chain | Residue |
| B | ARG98 |
| B | HOH701 |
| B | PRO27 |
| B | ASP28 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME B 509 |
| Chain | Residue |
| B | VAL261 |
| B | CYS262 |
| B | ASN263 |
| site_id | CC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MES B 510 |
| Chain | Residue |
| B | ALA44 |
| B | HIS45 |
| B | ASP47 |
| B | ALA48 |
| B | ALA325 |
| B | ARG348 |
| B | GLU352 |
| B | HOH618 |
| B | HOH646 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. AEAGGMSA |
| Chain | Residue | Details |
| A | ALA60-ALA67 |
