4A0M
CRYSTAL STRUCTURE OF BETAINE ALDEHYDE DEHYDROGENASE FROM SPINACH IN COMPLEX WITH NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006081 | biological_process | cellular aldehyde metabolic process |
| A | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| 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 | 0030955 | molecular_function | potassium ion binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| A | 0110095 | biological_process | cellular detoxification of aldehyde |
| B | 0006081 | biological_process | cellular aldehyde metabolic process |
| B | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| 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 | 0030955 | molecular_function | potassium ion binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| B | 0110095 | biological_process | cellular detoxification of aldehyde |
| C | 0006081 | biological_process | cellular aldehyde metabolic process |
| C | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| 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 | 0030955 | molecular_function | potassium ion binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| C | 0110095 | biological_process | cellular detoxification of aldehyde |
| D | 0006081 | biological_process | cellular aldehyde metabolic process |
| D | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| 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 | 0030955 | molecular_function | potassium ion binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| D | 0110095 | biological_process | cellular detoxification of aldehyde |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K D 1497 |
| Chain | Residue |
| D | ILE28 |
| D | ASP96 |
| D | LEU186 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K C 1497 |
| Chain | Residue |
| C | ILE28 |
| C | ASP96 |
| C | LEU186 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE K B 1497 |
| Chain | Residue |
| B | ASP96 |
| B | LEU186 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K A 1497 |
| Chain | Residue |
| A | ASP96 |
| A | LEU186 |
| A | ILE28 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD D 1498 |
| Chain | Residue |
| D | ILE155 |
| D | SER156 |
| D | PRO157 |
| D | TRP158 |
| D | ASN159 |
| D | LYS182 |
| D | SER184 |
| D | GLU185 |
| D | GLY215 |
| D | GLY219 |
| D | ALA220 |
| D | PHE233 |
| D | THR234 |
| D | GLY235 |
| D | SER236 |
| D | THR239 |
| D | GLU257 |
| D | LEU258 |
| D | GLY259 |
| D | CYS291 |
| D | GLU390 |
| D | PHE392 |
| D | LEU418 |
| D | TRP456 |
| D | HOH2045 |
| D | HOH2094 |
| D | HOH2095 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD C 1498 |
| Chain | Residue |
| C | ILE155 |
| C | SER156 |
| C | PRO157 |
| C | TRP158 |
| C | ASN159 |
| C | LYS182 |
| C | PRO183 |
| C | SER184 |
| C | GLU185 |
| C | GLY215 |
| C | GLY219 |
| C | ALA220 |
| C | PHE233 |
| C | THR234 |
| C | GLY235 |
| C | SER236 |
| C | THR239 |
| C | GLU257 |
| C | LEU258 |
| C | GLY259 |
| C | CYS291 |
| C | GLU390 |
| C | PHE392 |
| C | LEU418 |
| C | TRP456 |
| C | HOH2061 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD B 1498 |
| Chain | Residue |
| B | ILE155 |
| B | SER156 |
| B | PRO157 |
| B | TRP158 |
| B | ASN159 |
| B | LYS182 |
| B | PRO183 |
| B | SER184 |
| B | GLU185 |
| B | GLY215 |
| B | GLY219 |
| B | ALA220 |
| B | PHE233 |
| B | THR234 |
| B | GLY235 |
| B | SER236 |
| B | THR239 |
| B | GLU257 |
| B | GLY259 |
| B | CYS291 |
| B | GLU390 |
| B | PHE392 |
| B | TRP456 |
| B | HOH2062 |
| B | HOH2077 |
| B | HOH2083 |
| B | HOH2126 |
| B | HOH2127 |
| B | HOH2128 |
| D | GLU138 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 1498 |
| Chain | Residue |
| A | LYS182 |
| A | SER184 |
| A | GLU185 |
| A | GLY215 |
| A | GLY219 |
| A | ALA220 |
| A | PHE233 |
| A | THR234 |
| A | GLY235 |
| A | SER236 |
| A | THR239 |
| A | GLU257 |
| A | LEU258 |
| A | GLY259 |
| A | CYS291 |
| A | GLU390 |
| A | PHE392 |
| A | LEU418 |
| A | TRP456 |
| A | HOH2074 |
| A | HOH2166 |
| A | HOH2167 |
| A | HOH2168 |
| A | ILE155 |
| A | SER156 |
| A | PRO157 |
| A | TRP158 |
| A | ASN159 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 1499 |
| Chain | Residue |
| C | LEU477 |
| C | ASN478 |
| C | ILE479 |
| D | PHE464 |
| D | GLY465 |
| D | ARG466 |
| D | HOH2096 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 1500 |
| Chain | Residue |
| D | TYR160 |
| D | TRP167 |
| D | CYS291 |
| D | SER292 |
| D | GLN448 |
| D | CYS450 |
| D | GOL1501 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 1501 |
| Chain | Residue |
| D | ASP110 |
| D | CYS450 |
| D | PHE451 |
| D | GOL1500 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 1499 |
| Chain | Residue |
| C | ARG55 |
| C | PHE58 |
| C | LEU149 |
| C | GLY150 |
| C | ASP229 |
| C | HOH2129 |
| D | GLU438 |
| D | LYS460 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 1502 |
| Chain | Residue |
| C | LYS435 |
| C | GLU438 |
| D | GLN147 |
| D | PRO148 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1499 |
| Chain | Residue |
| A | TRP471 |
| A | GLN474 |
| B | ARG146 |
| B | GLN474 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1500 |
| Chain | Residue |
| A | GLN448 |
| A | CYS450 |
| A | HOH2170 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 1499 |
| Chain | Residue |
| A | VAL251 |
| A | PRO253 |
| A | HOH2070 |
| B | LYS460 |
| B | GLY463 |
| B | HOH2121 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 1501 |
| Chain | Residue |
| A | LYS460 |
| A | GLY463 |
| A | HOH2149 |
| B | VAL251 |
| B | PRO253 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 1500 |
| Chain | Residue |
| C | VAL251 |
| C | PRO253 |
| C | HOH2053 |
| D | LYS460 |
| D | GLY463 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 1501 |
| Chain | Residue |
| C | LYS460 |
| C | GLY463 |
| C | HOH2118 |
| D | VAL251 |
| D | PRO253 |
| D | HOH2053 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FwTNGQICSATS |
| Chain | Residue | Details |
| A | PHE284-SER295 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| A | LEU256-PRO263 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008 |
| Chain | Residue | Details |
| A | GLU257 | |
| B | GLU257 | |
| C | GLU257 | |
| D | GLU257 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000255|PROSITE-ProRule:PRU10008, ECO:0000305|PubMed:22345508 |
| Chain | Residue | Details |
| A | CYS291 | |
| B | CYS291 | |
| C | CYS291 | |
| D | CYS291 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22345508, ECO:0000269|PubMed:26792760, ECO:0007744|PDB:4A0M, ECO:0007744|PDB:5A2D |
| Chain | Residue | Details |
| A | ILE28 | |
| C | ASP96 | |
| C | LEU186 | |
| C | LYS460 | |
| D | ILE28 | |
| D | ASP96 | |
| D | LEU186 | |
| D | LYS460 | |
| A | ASP96 | |
| A | LEU186 | |
| A | LYS460 | |
| B | ILE28 | |
| B | ASP96 | |
| B | LEU186 | |
| B | LYS460 | |
| C | ILE28 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22345508, ECO:0007744|PDB:4A0M, ECO:0007744|PDB:4V37 |
| Chain | Residue | Details |
| A | SER156 | |
| B | TRP456 | |
| C | SER156 | |
| C | LYS182 | |
| C | SER236 | |
| C | GLU390 | |
| C | TRP456 | |
| D | SER156 | |
| D | LYS182 | |
| D | SER236 | |
| D | GLU390 | |
| A | LYS182 | |
| D | TRP456 | |
| A | SER236 | |
| A | GLU390 | |
| A | TRP456 | |
| B | SER156 | |
| B | LYS182 | |
| B | SER236 | |
| B | GLU390 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:22345508, ECO:0000269|PubMed:26792760, ECO:0007744|PDB:4A0M, ECO:0007744|PDB:5A2D |
| Chain | Residue | Details |
| A | VAL251 | |
| B | VAL251 | |
| C | VAL251 | |
| D | VAL251 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22345508, ECO:0007744|PDB:4V37 |
| Chain | Residue | Details |
| A | LEU258 | |
| B | LEU258 | |
| C | LEU258 | |
| D | LEU258 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P20000 |
| Chain | Residue | Details |
| A | ASN159 | |
| B | ASN159 | |
| C | ASN159 | |
| D | ASN159 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Blocked amino end (Arg) |
| Chain | Residue | Details |
| A | ARG8 | |
| B | ARG8 | |
| C | ARG8 | |
| D | ARG8 |
