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 | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007 |
Chain | Residue | Details |
A | GLU260 | |
B | GLU260 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10008 |
Chain | Residue | Details |
A | CYS294 | |
B | CYS294 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20026072, ECO:0007744|PDB:3IWJ |
Chain | Residue | Details |
A | ILE28 | |
B | LYS185 | |
B | LEU189 | |
B | SER239 | |
A | ASP99 | |
A | TRP161 | |
A | LYS185 | |
A | LEU189 | |
A | SER239 | |
B | ILE28 | |
B | ASP99 | |
B | TRP161 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P20000 |
Chain | Residue | Details |
A | ASN162 | |
B | ASN162 |