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 | 1-pyrroline-5-carboxylate 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 | proline biosynthetic process |
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 |
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 | 1-pyrroline-5-carboxylate 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 | proline biosynthetic process |
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 |
B | 0042802 | molecular_function | identical protein binding |
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 |