4NMB
Crystal structure of proline utilization A (PutA) from Geobacter sulfurreducens PCA in complex with L-lactate
Replaces: 4F9IFunctional 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 | 32 |
| 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 | ARG422 |
| A | GLU425 |
| A | SER431 |
| A | PHE432 |
| A | 2OP2002 |
| A | HOH2182 |
| A | VAL274 |
| A | HOH2188 |
| A | HOH2207 |
| A | HOH2379 |
| A | GLN276 |
| A | TYR278 |
| A | ARG303 |
| A | VAL305 |
| A | LYS306 |
| A | GLY307 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 2OP A 2002 |
| Chain | Residue |
| A | LYS203 |
| A | TYR418 |
| A | ARG421 |
| A | ARG422 |
| A | FAD2001 |
| A | HOH2207 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MES A 2003 |
| Chain | Residue |
| A | GLU609 |
| A | PHE613 |
| A | PHE656 |
| A | SER794 |
| A | GLY949 |
| A | ALA950 |
| A | PHE957 |
| A | HOH2240 |
| A | HOH2253 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD B 2001 |
| Chain | Residue |
| B | ASP244 |
| B | MET245 |
| 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 | TYR406 |
| B | ARG422 |
| B | GLU425 |
| B | SER431 |
| B | PHE432 |
| B | 2OP2002 |
| B | HOH2146 |
| B | HOH2201 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 2OP B 2002 |
| Chain | Residue |
| B | LYS203 |
| B | ALA308 |
| B | TYR418 |
| B | ARG421 |
| B | ARG422 |
| B | FAD2001 |
| B | HOH2188 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MES B 2003 |
| Chain | Residue |
| B | GLU609 |
| B | PHE613 |
| B | PHE656 |
| B | ILE660 |
| B | SER794 |
| B | THR948 |
| B | GLY949 |
| B | ALA950 |
| B | HOH2108 |
| B | HOH2253 |
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 |
