4I8P
Crystal structure of aminoaldehyde dehydrogenase 1a from Zea mays (ZmAMADH1a)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0031402 | molecular_function | sodium 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 | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| A | 0110095 | biological_process | cellular detoxification of aldehyde |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 | 0031402 | molecular_function | sodium 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 | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| B | 0110095 | biological_process | cellular detoxification of aldehyde |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD A 601 |
| Chain | Residue |
| A | ILE160 |
| A | GLY220 |
| A | GLY224 |
| A | ALA225 |
| A | PHE238 |
| A | THR239 |
| A | GLY240 |
| A | SER241 |
| A | THR244 |
| A | LYS247 |
| A | ILE248 |
| A | THR161 |
| A | GLU262 |
| A | LEU263 |
| A | GLY264 |
| A | CYS296 |
| A | GLU395 |
| A | PHE397 |
| A | LEU423 |
| A | TRP461 |
| A | HOH709 |
| A | HOH826 |
| A | PRO162 |
| A | HOH837 |
| A | HOH842 |
| A | HOH937 |
| A | HOH957 |
| A | HOH1085 |
| A | TRP163 |
| A | ASN164 |
| A | LYS187 |
| A | PRO188 |
| A | SER189 |
| A | GLU190 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 602 |
| Chain | Residue |
| A | VAL30 |
| A | ASP101 |
| A | LEU191 |
| A | HOH701 |
| A | HOH919 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 603 |
| Chain | Residue |
| A | PRO28 |
| A | GLU190 |
| A | LEU219 |
| A | HOH1021 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 604 |
| Chain | Residue |
| A | TRP172 |
| A | CYS296 |
| A | SER297 |
| A | HOH810 |
| A | HOH898 |
| site_id | AC5 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD B 601 |
| Chain | Residue |
| B | ILE160 |
| B | THR161 |
| B | PRO162 |
| B | TRP163 |
| B | ASN164 |
| B | LYS187 |
| B | PRO188 |
| B | SER189 |
| B | GLU190 |
| B | GLY220 |
| B | GLY224 |
| B | ALA225 |
| B | PHE238 |
| B | THR239 |
| B | GLY240 |
| B | SER241 |
| B | THR244 |
| B | ILE248 |
| B | GLU262 |
| B | LEU263 |
| B | GLY264 |
| B | CYS296 |
| B | GLU395 |
| B | PHE397 |
| B | TRP461 |
| B | HOH713 |
| B | HOH720 |
| B | HOH731 |
| B | HOH813 |
| B | HOH814 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 602 |
| Chain | Residue |
| B | VAL30 |
| B | ASP101 |
| B | LEU191 |
| B | HOH773 |
| B | HOH845 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG B 603 |
| Chain | Residue |
| B | LYS355 |
| B | ILE361 |
| B | GLY364 |
| B | GLY365 |
| B | HOH865 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 604 |
| Chain | Residue |
| B | TYR165 |
| B | TRP172 |
| B | TRP290 |
| B | CYS296 |
| B | SER297 |
| B | TRP461 |
| B | HOH921 |
| B | HOH981 |
| B | HOH1005 |
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 | PHE289-SER300 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| A | LEU261-PRO268 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23408433","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4I8P","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P20000","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
