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 | cellular 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 | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
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 | cellular 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 | 0043878 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity |
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 | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007 |
Chain | Residue | Details |
A | GLY296 | |
B | GLY296 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:26260980 |
Chain | Residue | Details |
A | ARG330 | |
B | ARG330 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20207735, ECO:0000269|PubMed:26260980, ECO:0007744|PDB:2J6L, ECO:0007744|PDB:4X0T, ECO:0007744|PDB:4ZUK, ECO:0007744|PDB:4ZVY |
Chain | Residue | Details |
A | ALA192 | |
A | ALA218 | |
A | VAL258 | |
A | ALA274 | |
B | ALA192 | |
B | ALA218 | |
B | VAL258 | |
B | ALA274 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20207735, ECO:0000269|PubMed:26260980, ECO:0007744|PDB:2J6L, ECO:0007744|PDB:4X0T |
Chain | Residue | Details |
A | GLY296 | |
A | LEU427 | |
B | GLY296 | |
B | LEU427 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0007744|PDB:4ZUL |
Chain | Residue | Details |
A | VAL331 | |
A | MET489 | |
A | ARG490 | |
B | VAL331 | |
B | MET489 | |
B | ARG490 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000250 |
Chain | Residue | Details |
A | THR195 | |
B | THR195 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DBF1 |
Chain | Residue | Details |
A | ARG94 | |
B | ARG94 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DBF1 |
Chain | Residue | Details |
A | ALA462 | |
A | LYS500 | |
B | ALA462 | |
B | LYS500 |