3IWK
Crystal structure of aminoaldehyde dehydrogenase 1 from Pisum sativum (PsAMADH1)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005777 | cellular_component | peroxisome |
| 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| A | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0031402 | molecular_function | sodium ion binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| A | 0110095 | biological_process | cellular detoxification of aldehyde |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005777 | cellular_component | peroxisome |
| 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| B | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0031402 | molecular_function | sodium ion binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| B | 0110095 | biological_process | cellular detoxification of aldehyde |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005777 | cellular_component | peroxisome |
| 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 |
| C | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| C | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| C | 0031402 | molecular_function | sodium ion binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| C | 0110095 | biological_process | cellular detoxification of aldehyde |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005777 | cellular_component | peroxisome |
| 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 |
| D | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| D | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| D | 0031402 | molecular_function | sodium ion binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| D | 0110095 | biological_process | cellular detoxification of aldehyde |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0005777 | cellular_component | peroxisome |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| E | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| E | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| E | 0031402 | molecular_function | sodium ion binding |
| E | 0042803 | molecular_function | protein homodimerization activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| E | 0110095 | biological_process | cellular detoxification of aldehyde |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0005777 | cellular_component | peroxisome |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| F | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| F | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| F | 0031402 | molecular_function | sodium ion binding |
| F | 0042803 | molecular_function | protein homodimerization activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| F | 0110095 | biological_process | cellular detoxification of aldehyde |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0005777 | cellular_component | peroxisome |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| G | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| G | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| G | 0031402 | molecular_function | sodium ion binding |
| G | 0042803 | molecular_function | protein homodimerization activity |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| G | 0110095 | biological_process | cellular detoxification of aldehyde |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0005777 | cellular_component | peroxisome |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| H | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| H | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| H | 0031402 | molecular_function | sodium ion binding |
| H | 0042803 | molecular_function | protein homodimerization activity |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| H | 0110095 | biological_process | cellular detoxification of aldehyde |
| I | 0000166 | molecular_function | nucleotide binding |
| I | 0005777 | cellular_component | peroxisome |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| I | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| I | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| I | 0031402 | molecular_function | sodium ion binding |
| I | 0042803 | molecular_function | protein homodimerization activity |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| I | 0110095 | biological_process | cellular detoxification of aldehyde |
| J | 0000166 | molecular_function | nucleotide binding |
| J | 0005777 | cellular_component | peroxisome |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| J | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| J | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| J | 0031402 | molecular_function | sodium ion binding |
| J | 0042803 | molecular_function | protein homodimerization activity |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| J | 0110095 | biological_process | cellular detoxification of aldehyde |
| K | 0000166 | molecular_function | nucleotide binding |
| K | 0005777 | cellular_component | peroxisome |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| K | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| K | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| K | 0031402 | molecular_function | sodium ion binding |
| K | 0042803 | molecular_function | protein homodimerization activity |
| K | 0046872 | molecular_function | metal ion binding |
| K | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| K | 0110095 | biological_process | cellular detoxification of aldehyde |
| L | 0000166 | molecular_function | nucleotide binding |
| L | 0005777 | cellular_component | peroxisome |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| L | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| L | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| L | 0031402 | molecular_function | sodium ion binding |
| L | 0042803 | molecular_function | protein homodimerization activity |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| L | 0110095 | biological_process | cellular detoxification of aldehyde |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 504 |
| Chain | Residue |
| A | ASN27 |
| A | ILE28 |
| A | ASP99 |
| A | LEU189 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD A 505 |
| Chain | Residue |
| A | ALA223 |
| A | GLY238 |
| A | SER239 |
| A | THR242 |
| A | LYS245 |
| A | LEU261 |
| A | GLY262 |
| A | CYS294 |
| A | GLN341 |
| A | GLU393 |
| A | PHE395 |
| A | HOH1411 |
| A | HOH1444 |
| A | PRO160 |
| A | TRP161 |
| A | GLY218 |
| A | HIS219 |
| A | GLY222 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 504 |
| Chain | Residue |
| B | ASN27 |
| B | ILE28 |
| B | ASP99 |
| B | LEU189 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAD B 505 |
| Chain | Residue |
| B | PRO160 |
| B | TRP161 |
| B | GLY218 |
| B | HIS219 |
| B | GLY222 |
| B | ALA223 |
| B | GLY238 |
| B | SER239 |
| B | THR242 |
| B | LYS245 |
| B | ILE246 |
| B | GLY262 |
| B | CYS294 |
| B | GLN341 |
| B | LYS344 |
| B | GLU393 |
| B | PHE395 |
| B | HOH1344 |
| B | HOH1801 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL B 2001 |
| Chain | Residue |
| B | TRP494 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 2002 |
| Chain | Residue |
| B | ASN162 |
| B | TYR163 |
| B | MET167 |
| B | TRP170 |
| B | ILE293 |
| B | CYS294 |
| B | SER295 |
| B | TRP459 |
| B | HOH1673 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA C 504 |
| Chain | Residue |
| C | ASN27 |
| C | ILE28 |
| C | ASP99 |
| C | LEU189 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD C 505 |
| Chain | Residue |
| C | PRO160 |
| C | TRP161 |
| C | GLU188 |
| C | GLY218 |
| C | GLY222 |
| C | ALA223 |
| C | GLY238 |
| C | SER239 |
| C | THR242 |
| C | LYS245 |
| C | ILE246 |
| C | GLY262 |
| C | CYS294 |
| C | GLN341 |
| C | LYS344 |
| C | GLU393 |
| C | PHE395 |
| C | HOH1327 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 2003 |
| Chain | Residue |
| C | TYR163 |
| C | MET167 |
| C | TRP170 |
| C | ILE293 |
| C | CYS294 |
| C | SER295 |
| C | TRP459 |
| C | HOH1671 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA D 504 |
| Chain | Residue |
| D | ASN27 |
| D | ASP99 |
| D | LEU189 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NAD D 505 |
| Chain | Residue |
| D | GLY218 |
| D | HIS219 |
| D | GLY222 |
| D | ALA223 |
| D | SER239 |
| D | THR242 |
| D | LYS245 |
| D | ILE246 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MRD D 2004 |
| Chain | Residue |
| D | ILE293 |
| D | CYS294 |
| D | GLN451 |
| D | SER453 |
| D | TRP459 |
| D | ASN162 |
| D | TYR163 |
| D | MET167 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA E 504 |
| Chain | Residue |
| E | ASN27 |
| E | ILE28 |
| E | ASP99 |
| E | LEU189 |
| site_id | BC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD E 505 |
| Chain | Residue |
| E | PRO160 |
| E | TRP161 |
| E | GLU188 |
| E | GLY218 |
| E | HIS219 |
| E | GLY222 |
| E | ALA223 |
| E | GLY238 |
| E | SER239 |
| E | THR242 |
| E | LYS245 |
| E | ILE246 |
| E | LEU261 |
| E | GLY262 |
| E | CYS294 |
| E | GLN341 |
| E | LYS344 |
| E | GLU393 |
| E | PHE395 |
| E | HOH1357 |
| E | HOH1443 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA F 504 |
| Chain | Residue |
| F | ASN27 |
| F | ASP99 |
| F | LEU189 |
| site_id | BC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD F 505 |
| Chain | Residue |
| F | PRO160 |
| F | TRP161 |
| F | GLY218 |
| F | HIS219 |
| F | GLY222 |
| F | ALA223 |
| F | GLY238 |
| F | SER239 |
| F | THR242 |
| F | LYS245 |
| F | LEU261 |
| F | GLY262 |
| F | CYS294 |
| F | GLN341 |
| F | LYS344 |
| F | GLU393 |
| F | PHE395 |
| F | HOH1345 |
| F | HOH1353 |
| F | HOH1427 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL F 2006 |
| Chain | Residue |
| F | ASN162 |
| F | TYR163 |
| F | MET167 |
| F | TRP170 |
| F | ILE293 |
| F | CYS294 |
| F | SER295 |
| F | TRP459 |
| F | HOH1448 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA G 504 |
| Chain | Residue |
| G | ASN27 |
| G | ILE28 |
| G | ASP99 |
| G | LEU189 |
| site_id | CC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD G 505 |
| Chain | Residue |
| G | PRO160 |
| G | TRP161 |
| G | GLU188 |
| G | GLY218 |
| G | HIS219 |
| G | GLY222 |
| G | ALA223 |
| G | GLY238 |
| G | SER239 |
| G | THR242 |
| G | LYS245 |
| G | CYS294 |
| G | GLN341 |
| G | LYS344 |
| G | GLU393 |
| G | PHE395 |
| G | HOH1331 |
| G | HOH1374 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL G 2007 |
| Chain | Residue |
| G | THR385 |
| G | ASP416 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL G 2009 |
| Chain | Residue |
| G | ASN162 |
| G | ILE293 |
| G | CYS294 |
| G | SER295 |
| G | TRP459 |
| G | HOH1678 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL G 2011 |
| Chain | Residue |
| G | ILE58 |
| G | GLY153 |
| G | ASP232 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA H 504 |
| Chain | Residue |
| H | ASN27 |
| H | ASP99 |
| H | LEU189 |
| H | HOH1206 |
| site_id | CC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAD H 505 |
| Chain | Residue |
| H | TRP161 |
| H | GLU188 |
| H | GLY218 |
| H | HIS219 |
| H | GLY222 |
| H | ALA223 |
| H | GLY238 |
| H | SER239 |
| H | THR242 |
| H | LYS245 |
| H | LEU261 |
| H | GLY262 |
| H | CYS294 |
| H | GLN341 |
| H | GLU393 |
| H | PHE395 |
| H | HOH550 |
| H | HOH1329 |
| H | HOH1389 |
| site_id | CC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL H 2010 |
| Chain | Residue |
| H | ASN162 |
| H | TYR163 |
| H | GLU260 |
| H | ILE293 |
| H | CYS294 |
| H | SER295 |
| H | TRP459 |
| H | HOH1233 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA I 504 |
| Chain | Residue |
| I | ASN27 |
| I | ILE28 |
| I | ASP99 |
| I | LEU189 |
| I | HOH1476 |
| site_id | CC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD I 505 |
| Chain | Residue |
| I | PRO160 |
| I | TRP161 |
| I | GLU188 |
| I | GLY218 |
| I | HIS219 |
| I | GLY222 |
| I | ALA223 |
| I | GLY238 |
| I | SER239 |
| I | THR242 |
| I | LYS245 |
| I | LEU261 |
| I | GLY262 |
| I | CYS294 |
| I | GLN341 |
| I | LYS344 |
| I | GLU393 |
| I | PHE395 |
| I | HOH1330 |
| I | HOH1333 |
| I | HOH1751 |
| site_id | DC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL I 2012 |
| Chain | Residue |
| I | ASN162 |
| I | TYR163 |
| I | ILE293 |
| I | CYS294 |
| I | SER295 |
| I | TRP459 |
| I | HOH1682 |
| site_id | DC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA J 504 |
| Chain | Residue |
| J | ASN27 |
| J | ASP99 |
| J | LEU189 |
| site_id | DC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAD J 505 |
| Chain | Residue |
| J | PRO160 |
| J | TRP161 |
| J | GLY218 |
| J | GLY222 |
| J | ALA223 |
| J | GLY238 |
| J | SER239 |
| J | THR242 |
| J | LYS245 |
| J | ILE246 |
| J | GLY262 |
| J | CYS294 |
| J | GLN341 |
| J | GLU393 |
| J | PHE395 |
| J | HOH1332 |
| site_id | DC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL J 2013 |
| Chain | Residue |
| J | GLU477 |
| site_id | DC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL J 2014 |
| Chain | Residue |
| J | ASN162 |
| J | TYR163 |
| J | TRP170 |
| J | GLU260 |
| J | ILE293 |
| J | CYS294 |
| J | SER295 |
| J | TRP459 |
| J | HOH1683 |
| site_id | DC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA K 504 |
| Chain | Residue |
| K | ASN27 |
| K | ASP99 |
| K | LEU189 |
| K | HOH1454 |
| site_id | DC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD K 505 |
| Chain | Residue |
| K | PRO160 |
| K | TRP161 |
| K | GLU188 |
| K | GLY218 |
| K | HIS219 |
| K | GLY222 |
| K | ALA223 |
| K | GLY238 |
| K | SER239 |
| K | THR242 |
| K | LYS245 |
| K | LEU261 |
| K | GLY262 |
| K | CYS294 |
| K | GLN341 |
| K | LYS344 |
| K | GLU393 |
| K | PHE395 |
| K | HOH746 |
| K | HOH1335 |
| K | HOH1446 |
| site_id | DC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL K 2016 |
| Chain | Residue |
| K | ASN162 |
| K | TYR163 |
| K | MET167 |
| K | ILE293 |
| K | CYS294 |
| K | SER295 |
| K | TRP459 |
| K | HOH1451 |
| site_id | DC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL K 2018 |
| Chain | Residue |
| K | ASN412 |
| K | ASN415 |
| K | ASP416 |
| K | HOH1929 |
| L | LYS61 |
| L | GOL2005 |
| site_id | EC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL K 2019 |
| Chain | Residue |
| K | GLU477 |
| L | GOL2000 |
| site_id | EC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA L 504 |
| Chain | Residue |
| L | ASN27 |
| L | ILE28 |
| L | ASP99 |
| L | LEU189 |
| site_id | EC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAD L 505 |
| Chain | Residue |
| L | PRO160 |
| L | TRP161 |
| L | GLU188 |
| L | GLY218 |
| L | HIS219 |
| L | GLY222 |
| L | ALA223 |
| L | GLY238 |
| L | SER239 |
| L | THR242 |
| L | LYS245 |
| L | ILE246 |
| L | GLY262 |
| L | CYS294 |
| L | GLN341 |
| L | GLU393 |
| L | PHE395 |
| L | HOH1368 |
| L | HOH1445 |
| site_id | EC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL L 2000 |
| Chain | Residue |
| K | GOL2019 |
| L | TRP474 |
| site_id | EC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL L 2005 |
| Chain | Residue |
| K | GLU408 |
| K | ILE411 |
| K | GOL2018 |
| L | ARG60 |
| L | LYS61 |
| site_id | EC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL L 2008 |
| Chain | Residue |
| L | ASN162 |
| L | TYR163 |
| L | TRP170 |
| L | GLU260 |
| L | ILE293 |
| L | CYS294 |
| L | SER295 |
| L | TRP459 |
| L | HOH1452 |
| site_id | EC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL L 2015 |
| Chain | Residue |
| L | GLU319 |
| L | ILE321 |
| L | ILE323 |
| L | HIS368 |
| site_id | EC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL L 2017 |
| Chain | Residue |
| K | ALA241 |
| L | GLN252 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfTNGQICSATS |
| Chain | Residue | Details |
| A | PHE287-SER298 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| A | LEU259-PRO266 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007 |
| Chain | Residue | Details |
| A | GLU260 | |
| J | GLU260 | |
| K | GLU260 | |
| L | GLU260 | |
| B | GLU260 | |
| C | GLU260 | |
| D | GLU260 | |
| E | GLU260 | |
| F | GLU260 | |
| G | GLU260 | |
| H | GLU260 | |
| I | GLU260 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10008 |
| Chain | Residue | Details |
| A | CYS294 | |
| J | CYS294 | |
| K | CYS294 | |
| L | CYS294 | |
| B | CYS294 | |
| C | CYS294 | |
| D | CYS294 | |
| E | CYS294 | |
| F | CYS294 | |
| G | CYS294 | |
| H | CYS294 | |
| I | CYS294 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 84 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20026072, ECO:0007744|PDB:3IWK |
| Chain | Residue | Details |
| A | ASN27 | |
| B | ASP99 | |
| B | LEU189 | |
| B | GLY238 | |
| B | CYS294 | |
| B | GLU393 | |
| C | ASN27 | |
| C | ILE28 | |
| C | ASP99 | |
| C | LEU189 | |
| C | GLY238 | |
| A | ILE28 | |
| C | CYS294 | |
| C | GLU393 | |
| D | ASN27 | |
| D | ILE28 | |
| D | ASP99 | |
| D | LEU189 | |
| D | GLY238 | |
| D | CYS294 | |
| D | GLU393 | |
| E | ASN27 | |
| A | ASP99 | |
| E | ILE28 | |
| E | ASP99 | |
| E | LEU189 | |
| E | GLY238 | |
| E | CYS294 | |
| E | GLU393 | |
| F | ASN27 | |
| F | ILE28 | |
| F | ASP99 | |
| F | LEU189 | |
| A | LEU189 | |
| F | GLY238 | |
| F | CYS294 | |
| F | GLU393 | |
| G | ASN27 | |
| G | ILE28 | |
| G | ASP99 | |
| G | LEU189 | |
| G | GLY238 | |
| G | CYS294 | |
| G | GLU393 | |
| A | GLY238 | |
| H | ASN27 | |
| H | ILE28 | |
| H | ASP99 | |
| H | LEU189 | |
| H | GLY238 | |
| H | CYS294 | |
| H | GLU393 | |
| I | ASN27 | |
| I | ILE28 | |
| I | ASP99 | |
| A | CYS294 | |
| I | LEU189 | |
| I | GLY238 | |
| I | CYS294 | |
| I | GLU393 | |
| J | ASN27 | |
| J | ILE28 | |
| J | ASP99 | |
| J | LEU189 | |
| J | GLY238 | |
| J | CYS294 | |
| A | GLU393 | |
| J | GLU393 | |
| K | ASN27 | |
| K | ILE28 | |
| K | ASP99 | |
| K | LEU189 | |
| K | GLY238 | |
| K | CYS294 | |
| K | GLU393 | |
| L | ASN27 | |
| L | ILE28 | |
| B | ASN27 | |
| L | ASP99 | |
| L | LEU189 | |
| L | GLY238 | |
| L | CYS294 | |
| L | GLU393 | |
| B | ILE28 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P20000 |
| Chain | Residue | Details |
| A | ASN162 | |
| J | ASN162 | |
| K | ASN162 | |
| L | ASN162 | |
| B | ASN162 | |
| C | ASN162 | |
| D | ASN162 | |
| E | ASN162 | |
| F | ASN162 | |
| G | ASN162 | |
| H | ASN162 | |
| I | ASN162 |
