3HAZ
Crystal structure of bifunctional proline utilization A (PutA) protein
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003677 | molecular_function | DNA 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 | 0006560 | biological_process | proline metabolic process |
| A | 0006561 | biological_process | obsolete proline biosynthetic process |
| 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 |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003677 | molecular_function | DNA 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 | 0006560 | biological_process | proline metabolic process |
| B | 0006561 | biological_process | obsolete proline biosynthetic process |
| 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 |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD A 2001 |
| Chain | Residue |
| A | ASP278 |
| A | ALA344 |
| A | TYR345 |
| A | TRP346 |
| A | PHE364 |
| A | THR365 |
| A | ARG366 |
| A | LYS367 |
| A | THR370 |
| A | ALA393 |
| A | THR394 |
| A | ALA279 |
| A | HIS395 |
| A | ASN396 |
| A | TYR441 |
| A | SER466 |
| A | PHE467 |
| A | SO41006 |
| A | HOH1076 |
| A | HOH1077 |
| A | HOH1078 |
| A | ALA310 |
| A | GLN312 |
| A | TYR314 |
| A | ARG339 |
| A | VAL341 |
| A | LYS342 |
| A | GLY343 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD A 2003 |
| Chain | Residue |
| A | ILE654 |
| A | SER655 |
| A | PRO656 |
| A | TRP657 |
| A | ASN658 |
| A | ILE663 |
| A | LYS681 |
| A | PRO682 |
| A | ALA683 |
| A | GLY714 |
| A | GLY717 |
| A | ALA718 |
| A | PHE731 |
| A | THR732 |
| A | GLY733 |
| A | SER734 |
| A | VAL737 |
| A | ILE741 |
| A | GLU758 |
| A | THR759 |
| A | GLY760 |
| A | CYS792 |
| A | GLU884 |
| A | PHE886 |
| A | PHE954 |
| A | HOH1336 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1000 |
| Chain | Residue |
| A | PHE659 |
| A | ARG791 |
| A | SER793 |
| A | ILE945 |
| A | GLY946 |
| A | ALA947 |
| A | HOH1148 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1001 |
| Chain | Residue |
| A | ARG366 |
| A | LYS367 |
| A | ALA368 |
| A | HOH1084 |
| A | HOH1301 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
| Chain | Residue |
| A | GLY570 |
| A | ARG624 |
| A | HOH1340 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1003 |
| Chain | Residue |
| A | SER585 |
| A | ARG586 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1004 |
| Chain | Residue |
| A | ARG475 |
| A | ARG475 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1005 |
| Chain | Residue |
| A | MET421 |
| A | GLY422 |
| A | GLU423 |
| A | ALA424 |
| A | HOH1373 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1006 |
| Chain | Residue |
| A | LYS237 |
| A | ALA344 |
| A | ARG456 |
| A | FAD2001 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1007 |
| Chain | Residue |
| A | TYR12 |
| A | ALA13 |
| A | ASP359 |
| A | VAL517 |
| A | GLU518 |
| A | ALA524 |
| A | HOH1157 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1008 |
| Chain | Residue |
| A | VAL517 |
| A | GLU518 |
| A | PHE519 |
| A | ASP603 |
| A | HOH1083 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1009 |
| Chain | Residue |
| A | ARG334 |
| A | HOH1011 |
| A | GLU256 |
| A | ALA297 |
| A | PRO299 |
| A | LYS302 |
| A | HIS332 |
| site_id | BC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD B 2002 |
| Chain | Residue |
| B | ASP278 |
| B | ALA279 |
| B | ALA310 |
| B | GLN312 |
| B | TYR314 |
| B | ARG339 |
| B | VAL341 |
| B | LYS342 |
| B | GLY343 |
| B | ALA344 |
| B | TYR345 |
| B | TRP346 |
| B | PHE364 |
| B | THR365 |
| B | ARG366 |
| B | LYS367 |
| B | THR370 |
| B | ALA393 |
| B | THR394 |
| B | HIS395 |
| B | ASN396 |
| B | LEU418 |
| B | TYR441 |
| B | SER466 |
| B | PHE467 |
| B | SO41005 |
| B | HOH1052 |
| B | HOH1090 |
| B | HOH1176 |
| site_id | BC5 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD B 2004 |
| Chain | Residue |
| B | ILE654 |
| B | SER655 |
| B | PRO656 |
| B | TRP657 |
| B | ASN658 |
| B | ILE663 |
| B | LYS681 |
| B | PRO682 |
| B | ALA683 |
| B | GLY714 |
| B | GLY717 |
| B | ALA718 |
| B | PHE731 |
| B | THR732 |
| B | GLY733 |
| B | SER734 |
| B | VAL737 |
| B | ILE741 |
| B | GLU758 |
| B | THR759 |
| B | GLY760 |
| B | CYS792 |
| B | GLU884 |
| B | PHE886 |
| B | PHE954 |
| B | HOH1265 |
| B | HOH1299 |
| B | HOH1301 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1000 |
| Chain | Residue |
| B | ARG366 |
| B | LYS367 |
| B | ALA368 |
| B | HOH1093 |
| B | HOH1094 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1001 |
| Chain | Residue |
| B | PHE659 |
| B | ARG791 |
| B | SER793 |
| B | ILE945 |
| B | GLY946 |
| B | ALA947 |
| B | HOH1011 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1002 |
| Chain | Residue |
| B | SER585 |
| B | ARG586 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1003 |
| Chain | Residue |
| B | ARG475 |
| B | ARG475 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1004 |
| Chain | Residue |
| B | GLY570 |
| B | ARG624 |
| B | HOH1290 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1005 |
| Chain | Residue |
| B | LYS237 |
| B | ALA344 |
| B | ARG456 |
| B | FAD2002 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1006 |
| Chain | Residue |
| B | TYR12 |
| B | LEU358 |
| B | ASP359 |
| B | VAL517 |
| B | GLU518 |
| B | ALA524 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1007 |
| Chain | Residue |
| B | ARG356 |
| B | VAL517 |
| B | GLU518 |
| B | PHE519 |
| B | HOH1092 |
| B | HOH1254 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1008 |
| Chain | Residue |
| A | HIS970 |
| A | ALA973 |
| A | HOH1451 |
| B | HIS970 |
| B | ALA973 |
| B | HOH1111 |
Functional Information from PROSITE/UniProt






