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 | 1-pyrroline-5-carboxylate dehydrogenase activity |
A | 0004657 | molecular_function | proline dehydrogenase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0006562 | biological_process | proline catabolic process |
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 | 0003700 | molecular_function | DNA-binding transcription factor activity |
B | 0003842 | molecular_function | 1-pyrroline-5-carboxylate dehydrogenase activity |
B | 0004657 | molecular_function | proline dehydrogenase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0006562 | biological_process | proline catabolic process |
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 | 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 |