4LIH
The crystal structure of Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase from Burkholderia cenocepacia J2315
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| 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 |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| 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 |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES A 501 |
| Chain | Residue |
| A | ASN168 |
| A | PHE169 |
| A | MET300 |
| A | CYS301 |
| A | THR302 |
| A | ASP456 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 501 |
| Chain | Residue |
| B | LYS228 |
| B | ILE251 |
| B | HOH811 |
| B | VAL164 |
| B | GLY224 |
| B | GLY227 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES B 502 |
| Chain | Residue |
| B | ASN168 |
| B | PHE169 |
| B | LEU172 |
| B | MET300 |
| B | CYS301 |
| B | THR302 |
| B | ASP456 |
| B | HOH874 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 501 |
| Chain | Residue |
| C | GLY224 |
| C | GLY227 |
| C | LYS228 |
| C | HOH705 |
| C | HOH776 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES C 502 |
| Chain | Residue |
| C | ASN168 |
| C | MET300 |
| C | CYS301 |
| C | THR302 |
| C | ASP456 |
| C | PHE465 |
| C | HOH662 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 501 |
| Chain | Residue |
| D | VAL164 |
| D | GLY224 |
| D | GLY227 |
| D | LYS228 |
| D | VAL247 |
| D | HOH685 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES D 502 |
| Chain | Residue |
| D | ASN168 |
| D | PHE169 |
| D | LEU172 |
| D | MET300 |
| D | CYS301 |
| D | THR302 |
| D | ASP456 |
| D | HOH979 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MES E 501 |
| Chain | Residue |
| E | ASN168 |
| E | PHE169 |
| E | MET300 |
| E | CYS301 |
| E | THR302 |
| E | ASP456 |
| E | PHE465 |
| E | HOH929 |
| E | HOH1039 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO F 501 |
| Chain | Residue |
| F | GLY224 |
| F | GLY227 |
| F | LYS228 |
| F | ILE251 |
| F | HOH690 |
| F | HOH833 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES F 502 |
| Chain | Residue |
| F | ASN168 |
| F | PHE169 |
| F | MET300 |
| F | CYS301 |
| F | THR302 |
| F | ASP456 |
| F | PHE465 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO G 501 |
| Chain | Residue |
| G | GLY224 |
| G | GLY227 |
| G | LYS228 |
| G | HOH769 |
| G | HOH781 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES G 502 |
| Chain | Residue |
| G | ASN168 |
| G | MET300 |
| G | CYS301 |
| G | THR302 |
| G | ASP456 |
| G | PHE465 |
| G | HOH683 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO H 501 |
| Chain | Residue |
| H | VAL164 |
| H | GLY224 |
| H | GLY227 |
| H | LYS228 |
| H | VAL247 |
| H | HOH743 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO H 502 |
| Chain | Residue |
| H | GLY140 |
| H | THR154 |
| H | ARG155 |
| H | HOH693 |
| H | HOH813 |
| site_id | BC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MES H 503 |
| Chain | Residue |
| H | HOH727 |
| H | HOH923 |
| H | ASN168 |
| H | PHE169 |
| H | LEU172 |
| H | MET300 |
| H | CYS301 |
| H | THR302 |
| H | ASP456 |
| H | PHE465 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FyNMGEMCTAGS |
| Chain | Residue | Details |
| A | PHE294-SER305 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| A | LEU265-PRO272 |
