3V9K
Crystal structure of mouse 1-pyrroline-5-carboxylate dehydrogenase complexed with the product glutamate
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 | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 564 |
Chain | Residue |
A | CYS421 |
A | ASN422 |
A | TYR428 |
A | GLU430 |
A | HOH607 |
B | PRO459 |
B | ASP461 |
B | LYS462 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 565 |
Chain | Residue |
A | SER409 |
A | PRO411 |
A | HOH918 |
B | ASP77 |
B | TYR96 |
B | ASP265 |
B | THR268 |
A | ARG408 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE GLU A 1517 |
Chain | Residue |
A | ASN211 |
A | PHE212 |
A | ILE215 |
A | LYS347 |
A | CYS348 |
A | SER349 |
A | THR511 |
A | GLY512 |
A | SER513 |
A | PHE520 |
A | HOH978 |
A | HOH980 |
A | HOH999 |
A | HOH1034 |
A | HOH1041 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE GLU B 1518 |
Chain | Residue |
B | ASN211 |
B | PHE212 |
B | ILE215 |
B | LYS347 |
B | CYS348 |
B | SER349 |
B | THR511 |
B | GLY512 |
B | SER513 |
B | PHE520 |
B | HOH948 |
B | HOH950 |
B | HOH981 |
B | HOH982 |
B | HOH1038 |
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 |