4PZ2
Structure of Zm ALDH2-6 (RF2F) in complex with NAD
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004029 | molecular_function | 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 |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004029 | molecular_function | 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 |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004029 | molecular_function | 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 |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004029 | molecular_function | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 601 |
Chain | Residue |
A | THR55 |
A | ARG56 |
A | ASP124 |
A | GLN211 |
A | HOH716 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG A 602 |
Chain | Residue |
A | SER49 |
A | GLY50 |
A | THR52 |
site_id | AC3 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD A 603 |
Chain | Residue |
A | ILE181 |
A | PRO182 |
A | TRP183 |
A | ASN184 |
A | MET189 |
A | LYS207 |
A | ALA209 |
A | GLU210 |
A | GLY240 |
A | GLY244 |
A | ALA245 |
A | PHE258 |
A | THR259 |
A | GLY260 |
A | SER261 |
A | VAL264 |
A | LEU267 |
A | ILE268 |
A | GLU283 |
A | LEU284 |
A | GLY285 |
A | CYS317 |
A | GLU417 |
A | PHE419 |
A | LEU445 |
A | PHE483 |
A | HOH710 |
A | ILE180 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO A 604 |
Chain | Residue |
A | MET477 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO A 605 |
Chain | Residue |
A | GLN326 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 606 |
Chain | Residue |
A | GLN166 |
A | HOH725 |
C | ASN458 |
D | GLN166 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA B 601 |
Chain | Residue |
B | THR55 |
B | ARG56 |
B | ASP124 |
B | GLN211 |
site_id | AC8 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD B 602 |
Chain | Residue |
B | ILE180 |
B | ILE181 |
B | PRO182 |
B | TRP183 |
B | ASN184 |
B | MET189 |
B | LYS207 |
B | ALA209 |
B | GLU210 |
B | GLY240 |
B | GLY244 |
B | ALA245 |
B | PHE258 |
B | THR259 |
B | GLY260 |
B | SER261 |
B | VAL264 |
B | LEU267 |
B | ILE268 |
B | GLU283 |
B | LEU284 |
B | GLY285 |
B | CYS317 |
B | GLU417 |
B | PHE419 |
B | PHE483 |
B | HOH704 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA C 601 |
Chain | Residue |
C | THR55 |
C | ARG56 |
C | ASP124 |
C | GLN211 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO C 602 |
Chain | Residue |
C | PHE483 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO C 603 |
Chain | Residue |
C | PHE293 |
C | GLN326 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO C 605 |
Chain | Residue |
C | GLN365 |
C | NAD606 |
site_id | BC4 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD C 606 |
Chain | Residue |
C | LEU267 |
C | ILE268 |
C | GLU283 |
C | LEU284 |
C | GLY285 |
C | CYS317 |
C | GLU417 |
C | PHE419 |
C | LEU445 |
C | PHE483 |
C | EDO605 |
C | HOH717 |
C | ILE180 |
C | ILE181 |
C | PRO182 |
C | TRP183 |
C | ASN184 |
C | MET189 |
C | LYS207 |
C | ALA209 |
C | GLU210 |
C | GLY240 |
C | GLY244 |
C | ALA245 |
C | PHE258 |
C | THR259 |
C | GLY260 |
C | SER261 |
C | VAL264 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA D 601 |
Chain | Residue |
D | THR55 |
D | ARG56 |
D | ASP124 |
D | GLN211 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO D 602 |
Chain | Residue |
D | GLY100 |
D | ALA104 |
site_id | BC7 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD D 603 |
Chain | Residue |
D | ILE180 |
D | ILE181 |
D | PRO182 |
D | TRP183 |
D | ASN184 |
D | MET189 |
D | LYS207 |
D | ALA209 |
D | GLU210 |
D | GLY240 |
D | GLY244 |
D | ALA245 |
D | PHE258 |
D | THR259 |
D | GLY260 |
D | SER261 |
D | VAL264 |
D | LEU267 |
D | ILE268 |
D | GLU283 |
D | LEU284 |
D | GLY285 |
D | CYS317 |
D | GLU417 |
D | PHE419 |
D | PHE483 |
Functional Information from PROSITE/UniProt
site_id | PS00070 |
Number of Residues | 12 |
Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNKGEACVAAS |
Chain | Residue | Details |
A | PHE310-SER321 |
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
Chain | Residue | Details |
A | LEU282-PRO289 |