4NMC
Crystal structure of oxidized proline utilization A (PutA) from Geobacter sulfurreducens PCA complexed with Zwittergent 3-12
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| A | 0004657 | molecular_function | proline dehydrogenase activity |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0006562 | biological_process | L-proline catabolic process |
| A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| A | 0010133 | biological_process | L-proline catabolic process to L-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 | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0003842 | molecular_function | L-glutamate gamma-semialdehyde dehydrogenase activity |
| B | 0004657 | molecular_function | proline dehydrogenase activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0006562 | biological_process | L-proline catabolic process |
| B | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
| B | 0010133 | biological_process | L-proline catabolic process to L-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 | 24 |
| Details | BINDING SITE FOR RESIDUE FAD A 2001 |
| Chain | Residue |
| A | ASP244 |
| A | ALA308 |
| A | TYR309 |
| A | TRP310 |
| A | TRP327 |
| A | THR328 |
| A | ILE329 |
| A | LYS330 |
| A | SER333 |
| A | ALA356 |
| A | SER357 |
| A | MET245 |
| A | HIS358 |
| A | ASN359 |
| A | LEU385 |
| A | TYR406 |
| A | HOH2579 |
| A | VAL274 |
| A | GLN276 |
| A | TYR278 |
| A | ARG303 |
| A | VAL305 |
| A | LYS306 |
| A | GLY307 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 A 2002 |
| Chain | Residue |
| A | HIS639 |
| A | HOH2536 |
| B | ARG933 |
| B | HOH2562 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 2003 |
| Chain | Residue |
| A | THR527 |
| A | VAL528 |
| A | GLU595 |
| A | ILE682 |
| A | HOH2119 |
| A | HOH2441 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD B 2001 |
| Chain | Residue |
| B | ASP244 |
| B | MET245 |
| B | VAL274 |
| B | GLN276 |
| B | TYR278 |
| B | ARG303 |
| B | VAL305 |
| B | LYS306 |
| B | GLY307 |
| B | ALA308 |
| B | TYR309 |
| B | TRP310 |
| B | TRP327 |
| B | THR328 |
| B | ILE329 |
| B | LYS330 |
| B | SER333 |
| B | ALA356 |
| B | SER357 |
| B | HIS358 |
| B | ASN359 |
| B | GLN383 |
| B | LEU385 |
| B | ARG422 |
| B | GLU425 |
| B | SER431 |
| B | PHE432 |
| B | 2OP2006 |
| B | HOH2170 |
| B | HOH2282 |
| B | HOH2461 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 B 2002 |
| Chain | Residue |
| A | HOH2236 |
| A | HOH2344 |
| B | LYS754 |
| B | VAL965 |
| B | HOH2220 |
| B | HOH2306 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 B 2003 |
| Chain | Residue |
| A | ARG933 |
| B | HIS639 |
| B | PHE641 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 2004 |
| Chain | Residue |
| B | THR527 |
| B | VAL528 |
| B | GLU595 |
| B | ILE682 |
| B | HOH2137 |
| B | HOH2359 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE C15 B 2005 |
| Chain | Residue |
| B | PHE76 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 2OP B 2006 |
| Chain | Residue |
| B | LYS203 |
| B | ALA308 |
| B | TYR418 |
| B | ARG421 |
| B | ARG422 |
| B | FAD2001 |
| B | HOH2182 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FgFQGQKCSACS |
| Chain | Residue | Details |
| A | PHE786-SER797 |
