2OPX
Crystal Structure of Lactaldehyde Dehydrogenase from Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004777 | molecular_function | succinate-semialdehyde dehydrogenase (NAD+) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0008911 | molecular_function | lactaldehyde dehydrogenase activity |
| A | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| 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 | 0019301 | biological_process | rhamnose catabolic process |
| A | 0019317 | biological_process | fucose catabolic process |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042355 | biological_process | L-fucose catabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0050569 | molecular_function | glycolaldehyde dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DXC A 1001 |
| Chain | Residue |
| A | PHE107 |
| A | ARG131 |
| A | PHE154 |
| A | ASN286 |
| A | PHE442 |
| A | GLU443 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE DXC A 1002 |
| Chain | Residue |
| A | GLU307 |
| A | PHE314 |
| A | GLY315 |
| A | ASN316 |
| A | ARG320 |
| A | ARG350 |
| A | TYR364 |
| A | LEU371 |
| A | HOH1249 |
| A | ASP299 |
| A | ASN303 |
| A | GLY306 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DXC A 1003 |
| Chain | Residue |
| A | ILE97 |
| A | ASN321 |
| A | ASP322 |
| A | ILE323 |
| A | ALA324 |
| A | HOH1213 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. ViNSGQVCNCAE |
| Chain | Residue | Details |
| A | VAL278-GLU289 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKAP |
| Chain | Residue | Details |
| A | LEU250-PRO257 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:17173928 |
| Chain | Residue | Details |
| A | CYS285 | |
| A | GLU251 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17173928, ECO:0007744|PDB:2IMP |
| Chain | Residue | Details |
| A | LYS176 | |
| A | GLN214 | |
| A | SER230 | |
| A | GLU251 | |
| A | ASN286 | |
| A | ARG336 | |
| A | GLU443 | |
| A | HIS449 | |
| A | LEU150 | |
| A | ARG161 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Important for substrate specificity => ECO:0000305|PubMed:27671251 |
| Chain | Residue | Details |
| A | ASN286 |
