4NMD
Crystal structure of proline utilization A (PutA) from Geobacter sulfurreducens PCA reduced with dithionite
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 | 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 | 27 |
Details | BINDING SITE FOR RESIDUE FDA A 1101 |
Chain | Residue |
A | ASP244 |
A | ALA308 |
A | TYR309 |
A | TRP310 |
A | TRP327 |
A | THR328 |
A | ILE329 |
A | LYS330 |
A | SER333 |
A | SER357 |
A | HIS358 |
A | MET245 |
A | ASN359 |
A | GLN383 |
A | VAL384 |
A | LEU385 |
A | TYR406 |
A | PHE432 |
A | HOH1355 |
A | HOH1495 |
A | VAL274 |
A | GLN276 |
A | TYR278 |
A | ARG303 |
A | VAL305 |
A | LYS306 |
A | GLY307 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 1102 |
Chain | Residue |
A | TYR248 |
A | TRP322 |
A | ASP485 |
A | THR487 |
A | HOH1204 |
A | HOH1471 |
A | HOH1613 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 1103 |
Chain | Residue |
A | TRP327 |
A | GLU332 |
A | ALA336 |
A | ARG339 |
A | ARG458 |
A | HOH1329 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1104 |
Chain | Residue |
A | TYR616 |
A | ARG619 |
A | GLU620 |
A | GLU953 |
A | HOH1644 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 1105 |
Chain | Residue |
A | GLU636 |
A | ASN987 |
B | GLN319 |
B | ARG945 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1106 |
Chain | Residue |
A | ASP770 |
A | ASP803 |
A | ALA804 |
A | LYS901 |
A | HOH1201 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 1107 |
Chain | Residue |
A | GLN319 |
A | ARG945 |
B | GLU636 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO A 1108 |
Chain | Residue |
A | GLU609 |
A | PHE613 |
A | ALA950 |
A | LEU951 |
A | VAL952 |
A | GLN955 |
A | PRO956 |
A | PHE957 |
A | ALA969 |
A | HOH1397 |
site_id | AC9 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FDA B 1101 |
Chain | Residue |
B | ASP244 |
B | MET245 |
B | VAL274 |
B | GLN276 |
B | TYR278 |
B | ARG303 |
B | LYS306 |
B | GLY307 |
B | ALA308 |
B | TYR309 |
B | TRP310 |
B | TRP327 |
B | THR328 |
B | ILE329 |
B | LYS330 |
B | SER333 |
B | SER357 |
B | HIS358 |
B | ASN359 |
B | GLN383 |
B | VAL384 |
B | LEU385 |
B | TYR406 |
B | GLU425 |
B | SER431 |
B | PHE432 |
B | HOH1547 |
B | HOH1548 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO B 1102 |
Chain | Residue |
B | VAL952 |
B | GLN955 |
B | PRO956 |
B | PHE957 |
B | ALA969 |
B | HOH1272 |
B | GLU609 |
B | PHE613 |
B | ALA950 |
B | LEU951 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 1103 |
Chain | Residue |
B | TYR248 |
B | TRP322 |
B | ASP485 |
B | HOH1215 |
B | HOH1316 |
B | HOH1328 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 1104 |
Chain | Residue |
B | TYR616 |
B | ARG619 |
B | GLU620 |
B | GLU953 |
B | HOH1658 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 1105 |
Chain | Residue |
A | GLU346 |
A | ASN347 |
B | ASP550 |
B | HOH1660 |
site_id | BC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO B 1106 |
Chain | Residue |
B | PHE513 |
B | GLY516 |
B | LEU699 |
B | PRO700 |
B | GLU701 |
B | GLY702 |
B | VAL703 |
B | PHE704 |
B | HOH1207 |
B | HOH1605 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 1107 |
Chain | Residue |
A | LYS755 |
B | LYS755 |
B | ILE756 |
B | VAL965 |
B | HIS977 |
B | HOH1283 |
site_id | BC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 1108 |
Chain | Residue |
B | ALA910 |
B | ASN911 |
B | THR913 |
B | PHE915 |
B | ALA916 |
B | ARG937 |
B | VAL938 |
B | HOH1247 |
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 |