4NMA
Crystal structure of proline utilization A (PutA) from Geobacter sulfurreducens PCA in complex with L-tetrahydro-2-furoic acid
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 | 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 | 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 | 29 |
| Details | BINDING SITE FOR RESIDUE FAD A 2001 |
| Chain | Residue |
| A | ASP244 |
| A | TYR309 |
| A | TRP310 |
| A | TRP327 |
| A | THR328 |
| A | ILE329 |
| A | LYS330 |
| A | SER333 |
| A | ALA356 |
| A | SER357 |
| A | HIS358 |
| A | MET245 |
| A | ASN359 |
| A | GLN383 |
| A | VAL384 |
| A | ARG422 |
| A | GLU425 |
| A | SER431 |
| A | PHE432 |
| A | TFB2002 |
| A | HOH2358 |
| A | HOH2434 |
| A | GLN276 |
| A | TYR278 |
| A | ARG303 |
| A | VAL305 |
| A | LYS306 |
| A | GLY307 |
| A | ALA308 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TFB A 2002 |
| Chain | Residue |
| A | LYS203 |
| A | ASP244 |
| A | ALA308 |
| A | TYR406 |
| A | TYR418 |
| A | ARG421 |
| A | ARG422 |
| A | FAD2001 |
| A | HOH2359 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 2003 |
| Chain | Residue |
| A | TYR248 |
| A | TRP322 |
| A | ASP485 |
| A | THR487 |
| A | HOH2259 |
| A | HOH2375 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 2004 |
| Chain | Residue |
| A | GLU609 |
| A | PHE613 |
| A | ALA950 |
| A | LEU951 |
| A | VAL952 |
| A | GLN955 |
| A | ALA969 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 2005 |
| Chain | Residue |
| A | ASN911 |
| A | THR913 |
| A | PHE915 |
| A | ARG937 |
| A | ARG961 |
| A | HOH2400 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 2006 |
| Chain | Residue |
| A | PRO269 |
| A | GLN299 |
| A | ILE300 |
| A | HIS352 |
| A | ARG379 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 2007 |
| Chain | Residue |
| A | TRP327 |
| A | GLU332 |
| A | ALA336 |
| A | ARG339 |
| A | HOH2287 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 2008 |
| Chain | Residue |
| A | GLY148 |
| A | GLU149 |
| A | THR151 |
| A | GLU156 |
| A | HOH2324 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 2009 |
| Chain | Residue |
| A | ARG619 |
| A | GLU620 |
| A | GLU953 |
| A | HOH2317 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 2010 |
| Chain | Residue |
| A | HIS498 |
| A | LYS583 |
| A | ARG584 |
| A | LEU585 |
| A | PHE586 |
| A | GLU587 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 2011 |
| Chain | Residue |
| A | LYS678 |
| A | GLY709 |
| A | GLY711 |
| A | HOH2258 |
| A | HOH2389 |
| A | HOH2436 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 2012 |
| Chain | Residue |
| A | ASP57 |
| A | PRO60 |
| A | SER61 |
| A | ARG924 |
| A | HOH2172 |
| B | ARG991 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 2013 |
| Chain | Residue |
| A | ASP770 |
| A | LEU802 |
| A | ASP803 |
| A | ALA804 |
| A | HOH2246 |
| site_id | BC5 |
| Number of Residues | 29 |
| 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 | LEU385 |
| B | ARG422 |
| B | GLU425 |
| B | SER431 |
| B | PHE432 |
| B | TFB2002 |
| B | HOH2106 |
| B | HOH2208 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TFB B 2002 |
| Chain | Residue |
| B | LYS203 |
| B | ASP244 |
| B | TYR406 |
| B | ARG421 |
| B | ARG422 |
| B | FAD2001 |
| B | HOH2149 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 2003 |
| Chain | Residue |
| B | ASP770 |
| B | ASP803 |
| B | ALA804 |
| B | LYS901 |
| B | HOH2122 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 2004 |
| Chain | Residue |
| B | GLU609 |
| B | PHE613 |
| B | ALA950 |
| B | LEU951 |
| B | GLN955 |
| B | PRO956 |
| B | PHE957 |
| B | ALA969 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 2005 |
| Chain | Residue |
| B | TYR248 |
| B | TRP322 |
| B | GLU323 |
| B | ASP485 |
| B | THR487 |
| B | HOH2374 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 2006 |
| Chain | Residue |
| A | GLN319 |
| A | ARG945 |
| B | GLU636 |
| B | ASN987 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 2007 |
| Chain | Residue |
| B | ALA910 |
| B | ASN911 |
| B | PHE915 |
| B | ARG937 |
| B | VAL938 |
| B | ARG961 |
| B | HOH2154 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 2008 |
| Chain | Residue |
| B | PRO269 |
| B | GLN299 |
| B | ILE300 |
| B | ILE350 |
| B | HIS352 |
| B | ARG379 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 2009 |
| Chain | Residue |
| B | TRP327 |
| B | GLU332 |
| B | ALA336 |
| B | ARG339 |
| B | ARG458 |
| site_id | CC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 2010 |
| Chain | Residue |
| B | PHE513 |
| B | LEU699 |
| B | PRO700 |
| B | GLU701 |
| B | GLY702 |
| B | VAL703 |
| B | PHE704 |
| B | HOH2204 |
| site_id | CC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 2011 |
| Chain | Residue |
| B | HIS498 |
| B | LYS583 |
| B | ARG584 |
| B | LEU585 |
| B | PHE586 |
| B | GLU587 |
| B | HOH2455 |
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 |
