4LH0
Structure of mouse 1-Pyrroline-5-Carboxylate Dehydrogenase (ALDH4A1) complexed with glyoxylate
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 | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| 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 |
| 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 | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| 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 |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLV A 601 |
| Chain | Residue |
| A | PHE212 |
| A | HOH1036 |
| A | SER349 |
| A | THR511 |
| A | GLY512 |
| A | SER513 |
| A | PHE520 |
| A | HOH991 |
| A | HOH993 |
| A | HOH1009 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1PE A 602 |
| Chain | Residue |
| A | ALA63 |
| A | TRP74 |
| A | TYR80 |
| A | LYS93 |
| B | THR61 |
| B | HOH712 |
| B | HOH1020 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GLV A 603 |
| Chain | Residue |
| A | GLU430 |
| A | HOH727 |
| B | LYS462 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GLV B 601 |
| Chain | Residue |
| B | PHE212 |
| B | SER349 |
| B | THR511 |
| B | GLY512 |
| B | SER513 |
| B | PHE520 |
| B | HOH995 |
| B | HOH996 |
| B | HOH1016 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 1PE B 602 |
| Chain | Residue |
| A | THR61 |
| A | HOH711 |
| A | HOH879 |
| A | HOH1052 |
| A | HOH1053 |
| B | ALA63 |
| B | TRP74 |
| B | TYR80 |
| B | LYS93 |
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, ECO:0000269|PubMed:22516612 |
| 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: |
| Chain | Residue | Details |
| A | GLY286 | |
| A | GLU447 | |
| A | SER513 | |
| B | SER208 | |
| B | LYS233 | |
| B | GLY286 | |
| B | GLU447 | |
| B | SER513 | |
| A | SER208 | |
| A | LYS233 |
| 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:0007744|PubMed:23806337 |
| Chain | Residue | Details |
| A | LYS395 | |
| B | LYS31 | |
| B | LYS347 | |
| B | LYS395 | |
| A | LYS31 | |
| A | LYS347 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P30038 |
| Chain | Residue | Details |
| A | SER44 | |
| B | SER44 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 14 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23576753 |
| Chain | Residue | Details |
| A | LYS552 | |
| B | LYS52 | |
| B | LYS318 | |
| B | LYS365 | |
| B | LYS376 | |
| B | LYS462 | |
| B | LYS531 | |
| B | LYS552 | |
| A | LYS52 | |
| A | LYS318 | |
| A | LYS365 | |
| A | LYS376 | |
| A | LYS462 | |
| A | LYS531 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 14 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 |
| Chain | Residue | Details |
| A | LYS114 | |
| A | LYS130 | |
| A | LYS175 | |
| A | LYS358 | |
| A | LYS509 | |
| B | LYS93 | |
| B | LYS99 | |
| B | LYS114 | |
| B | LYS130 | |
| B | LYS175 | |
| B | LYS358 | |
| B | LYS509 | |
| A | LYS93 | |
| A | LYS99 |
