2BJA
Crystal Analysis of 1-Pyrroline-5-Carboxylate Dehydrogenase from Thermus with bound NADH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
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 | 0000166 | molecular_function | nucleotide binding |
B | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
B | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
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 | 2 |
Details | BINDING SITE FOR RESIDUE CL A1519 |
Chain | Residue |
A | HIS465 |
B | LYS510 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B1519 |
Chain | Residue |
A | LYS510 |
B | HIS465 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE NAD A1517 |
Chain | Residue |
A | GLU210 |
A | GLY240 |
A | GLU241 |
A | ALA245 |
A | PHE258 |
A | SER261 |
A | VAL264 |
A | ACT1518 |
A | HOH2411 |
A | HOH2412 |
A | HOH2413 |
A | HOH2414 |
A | ILE180 |
A | ALA181 |
A | TRP183 |
A | LYS207 |
A | ALA209 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A1518 |
Chain | Residue |
A | ALA245 |
A | GLU249 |
A | LYS267 |
A | ALA271 |
A | NAD1517 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MRD A1520 |
Chain | Residue |
A | PHE6 |
A | TYR144 |
A | ARG147 |
A | ALA148 |
A | HOH2009 |
A | HOH2161 |
A | HOH2415 |
A | HOH2416 |
B | GLU158 |
B | VAL160 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NAD B1517 |
Chain | Residue |
B | ILE180 |
B | ALA181 |
B | TRP183 |
B | LYS207 |
B | ALA209 |
B | GLU210 |
B | GLY240 |
B | GLY244 |
B | ALA245 |
B | PHE258 |
B | SER261 |
B | VAL264 |
B | ACT1518 |
B | HOH2388 |
B | HOH2389 |
B | HOH2390 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B1518 |
Chain | Residue |
B | ALA245 |
B | GLU249 |
B | ILE268 |
B | ALA271 |
B | NAD1517 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MPD B1520 |
Chain | Residue |
A | GLU158 |
A | HOH2181 |
B | PHE6 |
B | TYR144 |
B | ARG147 |
B | ALA148 |
B | HOH2146 |
B | HOH2391 |
B | HOH2392 |
Functional Information from PROSITE/UniProt
site_id | PS00070 |
Number of Residues | 12 |
Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. YgFQGQKCSAAS |
Chain | Residue | Details |
A | TYR315-SER326 |
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. VETGGKDA |
Chain | Residue | Details |
A | VAL287-ALA294 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
A | ASN184 | |
A | GLU288 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
B | ASN184 | |
B | GLU288 |