4O6R
Crystal Structure of a Putative Aldehyde Dehydrogenase from Burkholderia cenocepacia
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 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 | 15 |
| Details | BINDING SITE FOR RESIDUE AMP A 501 |
| Chain | Residue |
| A | ILE145 |
| A | GLY225 |
| A | SER226 |
| A | THR229 |
| A | ARG232 |
| A | ILE233 |
| A | HOH902 |
| A | VAL146 |
| A | LYS172 |
| A | GLU175 |
| A | GLY205 |
| A | GLY209 |
| A | GLN210 |
| A | PHE223 |
| A | THR224 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NO3 A 502 |
| Chain | Residue |
| A | ARG104 |
| A | PHE150 |
| A | HIS275 |
| A | ALA280 |
| A | ILE282 |
| A | LYS440 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | HOH787 |
| A | HOH905 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 504 |
| Chain | Residue |
| A | ASP263 |
| A | ASN267 |
| A | ARG300 |
| A | HOH732 |
| A | HOH1026 |
| A | HOH1039 |
| A | HOH1135 |
| A | HOH1136 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NO3 A 505 |
| Chain | Residue |
| A | VAL126 |
| A | ASP127 |
| A | PHE130 |
| A | TRP475 |
| A | HOH897 |
| C | ARG441 |
| C | VAL442 |
| C | EDO507 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE AMP B 501 |
| Chain | Residue |
| B | ILE145 |
| B | VAL146 |
| B | LYS172 |
| B | GLU175 |
| B | GLY205 |
| B | GLY209 |
| B | GLN210 |
| B | PHE223 |
| B | THR224 |
| B | GLY225 |
| B | SER226 |
| B | THR229 |
| B | ARG232 |
| B | HOH881 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NO3 B 502 |
| Chain | Residue |
| B | ARG104 |
| B | PHE150 |
| B | HIS275 |
| B | ALA280 |
| B | ILE282 |
| B | LYS440 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| B | ASP263 |
| B | ASN267 |
| B | ARG300 |
| B | HOH749 |
| B | HOH796 |
| B | HOH1146 |
| B | HOH1147 |
| D | ARG488 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NO3 B 504 |
| Chain | Residue |
| B | VAL126 |
| B | ASP127 |
| B | PHE130 |
| B | TRP475 |
| B | HOH941 |
| D | ARG441 |
| D | VAL442 |
| D | ASN443 |
| D | EDO507 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NO3 C 501 |
| Chain | Residue |
| A | ARG441 |
| A | VAL442 |
| C | VAL126 |
| C | ASP127 |
| C | PHE130 |
| C | TRP475 |
| C | HOH722 |
| C | HOH819 |
| site_id | BC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AMP C 502 |
| Chain | Residue |
| C | HOH1125 |
| C | ILE145 |
| C | VAL146 |
| C | LYS172 |
| C | SER174 |
| C | GLU175 |
| C | GLY205 |
| C | GLY209 |
| C | GLN210 |
| C | PHE223 |
| C | GLY225 |
| C | SER226 |
| C | THR229 |
| C | ARG232 |
| C | HOH895 |
| C | HOH1124 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NO3 C 503 |
| Chain | Residue |
| C | ARG104 |
| C | PHE150 |
| C | HIS275 |
| C | ALA280 |
| C | ILE282 |
| C | LYS440 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 504 |
| Chain | Residue |
| C | LYS372 |
| C | LEU391 |
| C | ARG392 |
| C | HOH871 |
| C | HOH902 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 505 |
| Chain | Residue |
| C | ALA374 |
| C | THR375 |
| C | ALA401 |
| C | HOH884 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO C 506 |
| Chain | Residue |
| C | HOH982 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO C 507 |
| Chain | Residue |
| A | NO3505 |
| C | ARG104 |
| C | LYS440 |
| C | ARG441 |
| C | VAL442 |
| C | HOH733 |
| C | HOH927 |
| C | HOH1086 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 508 |
| Chain | Residue |
| A | HOH651 |
| C | ASP263 |
| C | ASN267 |
| C | ARG300 |
| C | HOH838 |
| C | HOH1141 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NO3 D 501 |
| Chain | Residue |
| B | ARG441 |
| B | VAL442 |
| B | ASN443 |
| D | VAL126 |
| D | ASP127 |
| D | PHE130 |
| D | TRP475 |
| D | HOH737 |
| D | HOH743 |
| site_id | CC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE AMP D 502 |
| Chain | Residue |
| D | ILE145 |
| D | VAL146 |
| D | LYS172 |
| D | SER174 |
| D | GLU175 |
| D | GLY205 |
| D | GLY209 |
| D | GLN210 |
| D | PHE223 |
| D | GLY225 |
| D | SER226 |
| D | THR229 |
| D | HOH876 |
| D | HOH1102 |
| D | HOH1114 |
| D | HOH1122 |
| D | HOH1123 |
| D | HOH1124 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NO3 D 503 |
| Chain | Residue |
| D | ARG104 |
| D | PHE150 |
| D | HIS275 |
| D | ALA280 |
| D | ILE282 |
| D | LYS440 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 504 |
| Chain | Residue |
| D | LYS372 |
| D | LEU391 |
| D | ARG392 |
| D | HOH808 |
| D | HOH874 |
| D | HOH1081 |
| site_id | CC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO D 505 |
| Chain | Residue |
| D | THR375 |
| D | HOH829 |
| site_id | CC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO D 506 |
| Chain | Residue |
| D | HOH908 |
| site_id | CC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 507 |
| Chain | Residue |
| B | NO3504 |
| D | ARG104 |
| D | TRP271 |
| D | LYS440 |
| D | ARG441 |
| D | VAL442 |
| D | HOH917 |
| D | HOH1027 |
| site_id | CC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 508 |
| Chain | Residue |
| B | HOH674 |
| D | ASP263 |
| D | ASN267 |
| D | ARG300 |
| D | HOH822 |
| D | HOH1137 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FhNQGQACIAGS |
| Chain | Residue | Details |
| A | PHE274-SER285 |
