4OE4
Crystal Structure of Yeast ALDH4A1 Complexed with NAD+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006537 | biological_process | glutamate biosynthetic process |
| A | 0006560 | biological_process | proline metabolic process |
| A | 0010133 | biological_process | proline catabolic process to glutamate |
| 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 | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006537 | biological_process | glutamate biosynthetic process |
| B | 0006560 | biological_process | proline metabolic process |
| B | 0010133 | biological_process | proline catabolic process to glutamate |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAD A 1000 |
| Chain | Residue |
| A | VAL208 |
| A | GLY287 |
| A | SER288 |
| A | VAL291 |
| A | GLY319 |
| A | GLU458 |
| A | PHE460 |
| A | HOH1102 |
| A | HOH1110 |
| A | HOH1116 |
| A | HOH1173 |
| A | SER209 |
| A | PRO210 |
| A | PHE211 |
| A | LYS234 |
| A | SER236 |
| A | PRO267 |
| A | THR271 |
| A | PHE285 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NAD B 1000 |
| Chain | Residue |
| B | VAL208 |
| B | SER209 |
| B | PRO210 |
| B | PHE211 |
| B | LYS234 |
| B | SER236 |
| B | PRO267 |
| B | VAL268 |
| B | THR271 |
| B | PHE285 |
| B | GLY287 |
| B | SER288 |
| B | VAL291 |
| B | LEU295 |
| B | HOH1109 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FeFQGQKCSAAS |
| Chain | Residue | Details |
| A | PHE344-SER355 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGKNF |
| Chain | Residue | Details |
| A | GLY316-PHE323 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 |
| Chain | Residue | Details |
| A | GLU317 | |
| B | GLU317 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 |
| Chain | Residue | Details |
| A | CYS351 | |
| B | CYS351 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY297 | |
| B | GLY297 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | ASN212 | |
| B | ASN212 |
