4E3X
Crystal Structure of Mus musculus 1-pyrroline-5-carboxylate dehydrogenase cryoprotected in proline
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 | 6 |
Details | BINDING SITE FOR RESIDUE PRO A 601 |
Chain | Residue |
A | LEU302 |
A | ASP303 |
A | PHE305 |
A | THR307 |
B | LYS292 |
B | ALA525 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PRO A 602 |
Chain | Residue |
A | LYS395 |
A | ALA396 |
A | ARG399 |
A | HOH867 |
A | PHE210 |
A | ILE392 |
A | ASP393 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PRO A 603 |
Chain | Residue |
A | SER41 |
A | GLN42 |
A | GLY43 |
A | SER44 |
A | PRO45 |
A | GLN184 |
A | PRO185 |
A | ILE186 |
A | HOH758 |
A | HOH930 |
A | HOH967 |
A | HOH1062 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PRO A 604 |
Chain | Residue |
A | CYS348 |
A | SER349 |
A | THR511 |
A | GLY512 |
A | SER513 |
A | PHE520 |
A | HOH855 |
A | HOH860 |
A | HOH1127 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 16P A 605 |
Chain | Residue |
A | THR61 |
A | TRP74 |
A | TYR80 |
A | LYS93 |
A | PGE606 |
B | THR61 |
B | LYS90 |
B | LYS93 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PGE A 606 |
Chain | Residue |
A | 16P605 |
B | LYS93 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PRO B 601 |
Chain | Residue |
A | LYS292 |
A | ALA525 |
B | LEU302 |
B | ASP303 |
B | PHE305 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PRO B 602 |
Chain | Residue |
B | PHE210 |
B | ILE392 |
B | ASP393 |
B | LYS395 |
B | ALA396 |
B | ARG399 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PRO B 603 |
Chain | Residue |
B | GLU165 |
B | PHE212 |
B | CYS348 |
B | SER349 |
B | THR511 |
B | GLY512 |
B | SER513 |
B | PHE520 |
B | HOH838 |
B | HOH839 |
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 | 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:0007744|PubMed:23806337 |
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: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 | 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 | 14 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 |
Chain | Residue | Details |
A | LYS93 | |
B | LYS114 | |
B | LYS130 | |
B | LYS175 | |
B | LYS358 | |
B | LYS509 | |
A | LYS99 | |
A | LYS114 | |
A | LYS130 | |
A | LYS175 | |
A | LYS358 | |
A | LYS509 | |
B | LYS93 | |
B | LYS99 |