8RKR
Structure of human DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE (ALDH4A1) complexed with a monophosphate-tweezer
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
| A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006560 | biological_process | proline metabolic process |
| A | 0006562 | biological_process | proline catabolic process |
| A | 0009055 | molecular_function | electron transfer activity |
| 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 |
| A | 0019470 | biological_process | 4-hydroxyproline catabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
| B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0006560 | biological_process | proline metabolic process |
| B | 0006562 | biological_process | proline catabolic process |
| B | 0009055 | molecular_function | electron transfer activity |
| 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 |
| B | 0019470 | biological_process | 4-hydroxyproline catabolic process |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FeYGGQKCSACS |
| Chain | Residue | Details |
| A | PHE341-SER352 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GECGGKNF |
| Chain | Residue | Details |
| A | GLY313-PHE320 |
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 | GLU314 | |
| B | GLU314 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008, ECO:0000269|PubMed:22516612 |
| Chain | Residue | Details |
| A | CYS348 | |
| B | CYS348 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER208 | |
| B | SER513 | |
| A | LYS233 | |
| A | GLY286 | |
| A | GLU447 | |
| A | SER513 | |
| B | SER208 | |
| B | LYS233 | |
| B | GLY286 | |
| B | GLU447 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | ASN211 | |
| B | ASN211 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8CHT0 |
| Chain | Residue | Details |
| A | LYS31 | |
| A | LYS347 | |
| A | LYS395 | |
| B | LYS31 | |
| B | LYS347 | |
| B | LYS395 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER44 | |
| B | SER44 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 14 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8CHT0 |
| Chain | Residue | Details |
| A | LYS52 | |
| B | LYS365 | |
| B | LYS376 | |
| B | LYS462 | |
| B | LYS531 | |
| B | LYS552 | |
| A | LYS318 | |
| A | LYS365 | |
| A | LYS376 | |
| A | LYS462 | |
| A | LYS531 | |
| A | LYS552 | |
| B | LYS52 | |
| B | LYS318 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q8CHT0 |
| Chain | Residue | Details |
| A | LYS93 | |
| B | LYS130 | |
| B | LYS175 | |
| B | LYS509 | |
| A | LYS99 | |
| A | LYS114 | |
| A | LYS130 | |
| A | LYS175 | |
| A | LYS509 | |
| B | LYS93 | |
| B | LYS99 | |
| B | LYS114 |
