4ZVY
Structure of human ALDH7A1 complexed with NAD+ in space group P4212
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| A | 0004043 | molecular_function | L-aminoadipate-semialdehyde dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006081 | biological_process | aldehyde metabolic process |
| A | 0007605 | biological_process | sensory perception of sound |
| A | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) 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 | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0042426 | biological_process | choline catabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| B | 0004043 | molecular_function | L-aminoadipate-semialdehyde dehydrogenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0006081 | biological_process | aldehyde metabolic process |
| B | 0007605 | biological_process | sensory perception of sound |
| B | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) 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 | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0042426 | biological_process | choline catabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue NAD B 601 |
| Chain | Residue |
| B | ILE163 |
| B | PHE244 |
| B | SER247 |
| B | VAL250 |
| B | VAL254 |
| B | HOH726 |
| B | THR164 |
| B | LYS190 |
| B | GLY191 |
| B | ALA192 |
| B | PRO193 |
| B | ALA227 |
| B | GLY230 |
| B | THR231 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGNNA |
| Chain | Residue | Details |
| A | LEU267-ALA274 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"26260980","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20207735","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26260980","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J6L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X0T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ZUK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ZVY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20207735","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26260980","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J6L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X0T","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4ZUL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9DBF1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DBF1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
