3IWJ
Crystal structure of aminoaldehyde dehydrogenase 2 from Pisum sativum (PsAMADH2)
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAD A 504 |
| Chain | Residue |
| A | ILE158 |
| A | ALA223 |
| A | PHE236 |
| A | GLY238 |
| A | SER239 |
| A | THR242 |
| A | ILE246 |
| A | HOH555 |
| A | HOH580 |
| A | THR159 |
| A | TRP161 |
| A | LYS185 |
| A | PRO186 |
| A | SER187 |
| A | GLU188 |
| A | GLY218 |
| A | GLY222 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 505 |
| Chain | Residue |
| A | ILE28 |
| A | ASP99 |
| A | LEU189 |
| A | HOH562 |
| A | HOH572 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 506 |
| Chain | Residue |
| A | ASP110 |
| A | ASP113 |
| A | CYS453 |
| A | HOH602 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 507 |
| Chain | Residue |
| A | ASN162 |
| A | TYR163 |
| A | TRP170 |
| A | ILE293 |
| A | CYS294 |
| A | TRP459 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 508 |
| Chain | Residue |
| A | GLU473 |
| A | ASP477 |
| B | ARG149 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAD B 504 |
| Chain | Residue |
| B | ILE158 |
| B | THR159 |
| B | TRP161 |
| B | LYS185 |
| B | PRO186 |
| B | SER187 |
| B | GLU188 |
| B | GLY218 |
| B | GLY222 |
| B | ALA223 |
| B | PHE236 |
| B | SER239 |
| B | THR242 |
| B | ILE246 |
| B | HOH544 |
| B | HOH575 |
| B | HOH610 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 505 |
| Chain | Residue |
| B | ILE28 |
| B | ASP99 |
| B | LEU189 |
| B | HOH526 |
| B | HOH537 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 506 |
| Chain | Residue |
| B | ASP113 |
| B | TYR163 |
| B | LEU166 |
| B | CYS453 |
| B | GOL508 |
| B | HOH658 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 507 |
| Chain | Residue |
| A | ARG149 |
| A | HOH599 |
| B | GLU473 |
| B | TRP474 |
| B | ASP477 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 508 |
| Chain | Residue |
| B | TYR163 |
| B | TRP170 |
| B | ILE293 |
| B | CYS294 |
| B | SER295 |
| B | TRP459 |
| B | GOL506 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 509 |
| Chain | Residue |
| B | LYS44 |
| B | THR227 |
| B | HOH590 |
| B | HOH618 |
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 | 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 | 4 |
| Details | Motif: {"description":"Microbody targeting signal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| 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_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20026072","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3IWJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P20000","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
