6POP
Crystal structure of DauA in complex with NADP+
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 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 | 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 |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 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 | 30 |
Details | binding site for residue NAP A 501 |
Chain | Residue |
A | PHE144 |
A | ASP209 |
A | LEU222 |
A | ILE223 |
A | GLY224 |
A | SER225 |
A | VAL228 |
A | HIS231 |
A | GLU246 |
A | LEU247 |
A | GLY248 |
A | LEU145 |
A | GLY249 |
A | CYS280 |
A | GLU378 |
A | LEU406 |
A | HIS443 |
A | EDO504 |
A | HOH609 |
A | HOH617 |
A | HOH669 |
A | HOH678 |
A | TRP147 |
A | HOH681 |
A | ASN148 |
A | LYS171 |
A | SER173 |
A | SER174 |
A | ASP204 |
A | GLY208 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | ASN440 |
A | LEU457 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | NAP501 |
A | HOH607 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | ILE22 |
A | PRO24 |
A | MET323 |
A | ASP324 |
A | TYR358 |
A | HOH622 |
site_id | AC5 |
Number of Residues | 34 |
Details | binding site for residue NAP B 501 |
Chain | Residue |
B | PHE144 |
B | LEU145 |
B | ALA146 |
B | TRP147 |
B | ASN148 |
B | LYS171 |
B | SER173 |
B | SER174 |
B | ASP204 |
B | GLY208 |
B | ASP209 |
B | LEU222 |
B | ILE223 |
B | GLY224 |
B | SER225 |
B | VAL228 |
B | HIS231 |
B | GLU246 |
B | LEU247 |
B | GLY248 |
B | GLY249 |
B | CYS280 |
B | GLU378 |
B | PHE380 |
B | HIS443 |
B | MG503 |
B | HOH605 |
B | HOH615 |
B | HOH617 |
B | HOH627 |
B | HOH629 |
B | HOH641 |
B | HOH643 |
B | HOH661 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
B | LEU152 |
B | TYR156 |
B | TYR437 |
B | HIS443 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue MG B 503 |
Chain | Residue |
B | NAP501 |
B | HOH605 |
B | HOH615 |
B | HOH635 |
B | HOH643 |
B | HOH661 |
site_id | AC8 |
Number of Residues | 34 |
Details | binding site for residue NAP C 501 |
Chain | Residue |
C | HIS231 |
C | GLU246 |
C | LEU247 |
C | GLY248 |
C | GLY249 |
C | CYS280 |
C | GLU378 |
C | LEU406 |
C | HIS443 |
C | MG502 |
C | HOH604 |
C | HOH607 |
C | HOH611 |
C | HOH612 |
C | HOH635 |
C | HOH639 |
C | HOH640 |
C | HOH670 |
C | HOH683 |
C | PHE144 |
C | LEU145 |
C | TRP147 |
C | ASN148 |
C | LYS171 |
C | SER173 |
C | SER174 |
C | ASP204 |
C | GLY208 |
C | ASP209 |
C | LEU222 |
C | ILE223 |
C | GLY224 |
C | SER225 |
C | VAL228 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MG C 502 |
Chain | Residue |
C | NAP501 |
C | HOH604 |
C | HOH639 |
C | HOH670 |
C | HOH683 |
C | HOH699 |
site_id | AD1 |
Number of Residues | 32 |
Details | binding site for residue NAP D 501 |
Chain | Residue |
D | PHE144 |
D | LEU145 |
D | TRP147 |
D | ASN148 |
D | LYS171 |
D | SER173 |
D | SER174 |
D | ASP204 |
D | GLY208 |
D | ASP209 |
D | LEU222 |
D | ILE223 |
D | GLY224 |
D | SER225 |
D | VAL228 |
D | HIS231 |
D | GLU246 |
D | LEU247 |
D | GLY248 |
D | CYS280 |
D | GLU378 |
D | PHE380 |
D | HIS443 |
D | EDO504 |
D | HOH604 |
D | HOH605 |
D | HOH611 |
D | HOH620 |
D | HOH623 |
D | HOH633 |
D | HOH665 |
D | HOH666 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue EDO D 502 |
Chain | Residue |
C | ILE122 |
D | SER456 |
D | LEU457 |
D | LEU458 |
D | HOH610 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue EDO D 503 |
Chain | Residue |
D | TYR156 |
D | TYR437 |
D | HOH649 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue EDO D 504 |
Chain | Residue |
D | SER225 |
D | VAL228 |
D | NAP501 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue EDO D 505 |
Chain | Residue |
D | THR226 |
D | ALA404 |
site_id | AD6 |
Number of Residues | 29 |
Details | binding site for residue NAP E 501 |
Chain | Residue |
E | LEU145 |
E | ALA146 |
E | TRP147 |
E | ASN148 |
E | LYS171 |
E | SER173 |
E | SER174 |
E | ASP204 |
E | GLY208 |
E | ASP209 |
E | LEU222 |
E | ILE223 |
E | GLY224 |
E | SER225 |
E | VAL228 |
E | HIS231 |
E | GLU246 |
E | LEU247 |
E | GLY248 |
E | GLY249 |
E | CYS280 |
E | GLU378 |
E | PHE380 |
E | HIS443 |
E | HOH605 |
E | HOH625 |
E | HOH632 |
E | HOH636 |
E | HOH639 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue EDO E 502 |
Chain | Residue |
E | TYR156 |
E | VAL281 |
E | TYR437 |
E | HIS443 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue EDO E 503 |
Chain | Residue |
E | ARG63 |
E | ILE114 |
E | ARG135 |
site_id | AD9 |
Number of Residues | 30 |
Details | binding site for residue NAP F 501 |
Chain | Residue |
F | PHE144 |
F | LEU145 |
F | ALA146 |
F | TRP147 |
F | ASN148 |
F | LYS171 |
F | SER173 |
F | SER174 |
F | ASP204 |
F | GLY208 |
F | ASP209 |
F | LEU222 |
F | ILE223 |
F | GLY224 |
F | SER225 |
F | VAL228 |
F | HIS231 |
F | GLU246 |
F | LEU247 |
F | GLY248 |
F | CYS280 |
F | GLU378 |
F | PHE380 |
F | HIS443 |
F | HOH615 |
F | HOH633 |
F | HOH639 |
F | HOH643 |
F | HOH653 |
F | HOH672 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue EDO F 502 |
Chain | Residue |
F | TYR156 |
F | HIS443 |
site_id | AE2 |
Number of Residues | 2 |
Details | binding site for residue EDO F 503 |
Chain | Residue |
F | THR226 |
F | ASP403 |
Functional Information from PROSITE/UniProt
site_id | PS00687 |
Number of Residues | 8 |
Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGNAP |
Chain | Residue | Details |
A | MET245-PRO252 |