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 |