2IMP
Crystal structure of lactaldehyde dehydrogenase from E. coli: the ternary complex with lactate (occupancy 0.5) and NADH. Crystals soaked with (L)-Lactate.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004030 | molecular_function | aldehyde dehydrogenase [NAD(P)+] activity |
| A | 0004777 | molecular_function | succinate-semialdehyde dehydrogenase (NAD+) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) activity |
| A | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| A | 0016052 | biological_process | carbohydrate 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 | 0044281 | biological_process | small molecule metabolic process |
| A | 0050569 | molecular_function | glycolaldehyde dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 509 |
| Chain | Residue |
| A | GLY254 |
| A | HOH656 |
| A | LYS255 |
| A | ALA256 |
| A | PRO257 |
| A | TYR409 |
| A | GLY410 |
| A | LEU411 |
| A | THR412 |
| A | PHE432 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 510 |
| Chain | Residue |
| A | SER70 |
| A | ARG73 |
| A | HOH532 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAI A 506 |
| Chain | Residue |
| A | ILE149 |
| A | LEU150 |
| A | PRO151 |
| A | TRP152 |
| A | LYS176 |
| A | SER178 |
| A | GLU179 |
| A | PHE180 |
| A | GLY209 |
| A | GLY213 |
| A | GLN214 |
| A | MET227 |
| A | GLY229 |
| A | SER230 |
| A | ALA233 |
| A | LYS236 |
| A | ILE237 |
| A | GLY253 |
| A | GLY254 |
| A | LYS255 |
| A | VAL284 |
| A | CYS285 |
| A | GLU289 |
| A | ASN330 |
| A | ALA332 |
| A | ARG336 |
| A | GLU383 |
| A | HOH628 |
| A | HOH638 |
| A | HOH645 |
| A | HOH715 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LAC A 508 |
| Chain | Residue |
| A | PHE154 |
| A | ARG161 |
| A | GLU251 |
| A | CYS285 |
| A | ASN286 |
| A | GLU443 |
| A | HIS449 |
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 | Active site: {"evidences":[{"source":"PubMed","id":"17173928","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17173928","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2IMP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for substrate specificity","evidences":[{"source":"PubMed","id":"27671251","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| A | CYS285 | |
| A | GLU251 | |
| A | ASN153 |
