6BSN
Structure of proline utilization A (PutA) with proline bound in remote sites
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 | 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 |
| A | 0055129 | biological_process | L-proline biosynthetic process |
| 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 | 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 |
| B | 0055129 | biological_process | L-proline biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | binding site for residue FDA 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 | SO42012 |
| A | HOH2268 |
| A | HOH2296 |
| A | ALA310 |
| A | GLN312 |
| A | TYR314 |
| A | ARG339 |
| A | VAL341 |
| A | LYS342 |
| A | GLY343 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue PRO A 2002 |
| Chain | Residue |
| A | ARG791 |
| A | SER793 |
| A | ILE945 |
| A | GLY946 |
| A | ALA947 |
| A | PHE954 |
| A | HOH2144 |
| A | HOH2234 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue PRO A 2003 |
| Chain | Residue |
| A | ALA973 |
| A | ARG974 |
| A | ALA976 |
| B | PRO964 |
| B | HIS970 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue PRO A 2004 |
| Chain | Residue |
| A | ASN3 |
| A | ILE4 |
| A | LYS820 |
| A | HOH2125 |
| A | HOH2267 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue PRO A 2005 |
| Chain | Residue |
| A | ARG284 |
| A | HOH2193 |
| A | HOH2239 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue PRO A 2006 |
| Chain | Residue |
| A | TRP657 |
| A | ASN658 |
| A | GLY733 |
| A | SER734 |
| A | PHE886 |
| A | HOH2335 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 2007 |
| Chain | Residue |
| A | ARG366 |
| A | LYS367 |
| A | ALA368 |
| A | HOH2156 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 2008 |
| Chain | Residue |
| A | MET421 |
| A | GLY422 |
| A | GLU423 |
| A | ALA424 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 2009 |
| Chain | Residue |
| A | ARG512 |
| A | HIS581 |
| A | ARG617 |
| A | HOH2107 |
| A | HOH2323 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 2010 |
| Chain | Residue |
| A | GLY570 |
| A | ARG624 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 2011 |
| Chain | Residue |
| A | SER585 |
| A | ARG586 |
| A | HOH2394 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 2012 |
| Chain | Residue |
| A | ASP193 |
| A | LYS237 |
| A | ALA344 |
| A | ARG456 |
| A | FDA2001 |
| A | HOH2116 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 2013 |
| Chain | Residue |
| A | THR348 |
| A | ARG352 |
| site_id | AD5 |
| Number of Residues | 28 |
| Details | binding site for residue FDA B 1001 |
| Chain | Residue |
| B | HIS395 |
| B | ASN396 |
| B | ARG417 |
| B | TYR441 |
| B | GLU460 |
| B | SER466 |
| B | PHE467 |
| B | SO41010 |
| B | HOH1170 |
| 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 |
| site_id | AD6 |
| Number of Residues | 9 |
| Details | binding site for residue PRO B 1002 |
| Chain | Residue |
| B | PHE659 |
| B | ARG791 |
| B | SER793 |
| B | ILE945 |
| B | GLY946 |
| B | ALA947 |
| B | PHE954 |
| B | HOH1124 |
| B | HOH1218 |
| site_id | AD7 |
| Number of Residues | 9 |
| Details | binding site for residue PRO B 1003 |
| Chain | Residue |
| A | PRO964 |
| A | HIS970 |
| B | MET645 |
| B | ARG648 |
| B | ALA973 |
| B | ARG974 |
| B | ALA976 |
| B | GLU978 |
| B | HOH1182 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue PRO B 1004 |
| Chain | Residue |
| B | ARG244 |
| B | PHE245 |
| B | GLU246 |
| B | ARG284 |
| B | HOH1257 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue PRO B 1005 |
| Chain | Residue |
| B | TRP657 |
| B | ASN658 |
| B | GLY733 |
| B | SO41011 |
| B | HOH1167 |
| B | HOH1249 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 1006 |
| Chain | Residue |
| B | ARG366 |
| B | LYS367 |
| B | ALA368 |
| B | HOH1304 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 1007 |
| Chain | Residue |
| B | MET421 |
| B | GLY422 |
| B | GLU423 |
| B | ALA424 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 1008 |
| Chain | Residue |
| B | ARG512 |
| B | HIS581 |
| B | ARG617 |
| B | HOH1292 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 1009 |
| Chain | Residue |
| B | LEU582 |
| B | SER585 |
| B | ARG586 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 1010 |
| Chain | Residue |
| B | ASP193 |
| B | LYS237 |
| B | ALA344 |
| B | ARG456 |
| B | FDA1001 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 1011 |
| Chain | Residue |
| B | TRP657 |
| B | GLN685 |
| B | PRO1005 |
| B | HOH1167 |
| site_id | AE7 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 1012 |
| Chain | Residue |
| B | THR348 |
| B | ARG352 |
Functional Information from PROSITE/UniProt
| site_id | PS00678 |
| Number of Residues | 15 |
| Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. IAATlaDpSLKGWDG |
| Chain | Residue | Details |
| A | ILE292-GLY306 |
