5VOH
Crystal structure of engineered water-forming NADPH oxidase (TPNOX) bound to NADPH. The G159A, D177A, A178R, M179S, P184R mutant of LbNOX.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0016491 | molecular_function | oxidoreductase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0016491 | molecular_function | oxidoreductase activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0016491 | molecular_function | oxidoreductase activity |
D | 0000166 | molecular_function | nucleotide binding |
D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 36 |
Details | binding site for residue FAD A 501 |
Chain | Residue |
A | GLY7 |
A | CSO42 |
A | HIS77 |
A | ASN78 |
A | VAL79 |
A | THR110 |
A | SER111 |
A | GLY112 |
A | SER113 |
A | CYS131 |
A | LYS132 |
A | THR9 |
A | ILE158 |
A | PHE242 |
A | ASN245 |
A | LEU248 |
A | GLY278 |
A | ASP279 |
A | PRO295 |
A | LEU296 |
A | ALA297 |
A | ALA300 |
A | HIS10 |
A | NDP502 |
A | HOH609 |
A | HOH620 |
A | HOH623 |
A | HOH634 |
A | HOH645 |
B | PHE422 |
A | ALA11 |
A | TYR31 |
A | GLU32 |
A | ARG33 |
A | ASN34 |
A | SER41 |
site_id | AC2 |
Number of Residues | 23 |
Details | binding site for residue NDP A 502 |
Chain | Residue |
A | GLY154 |
A | ALA155 |
A | GLY156 |
A | TYR157 |
A | ILE158 |
A | GLU161 |
A | ARG178 |
A | SER179 |
A | ARG184 |
A | LYS185 |
A | TYR186 |
A | CYS239 |
A | ILE240 |
A | GLY241 |
A | PHE242 |
A | PRO295 |
A | LEU296 |
A | SER325 |
A | GLY326 |
A | FAD501 |
A | SO4505 |
A | HOH642 |
B | HOH610 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | ARG332 |
A | LEU372 |
A | MET390 |
A | SER391 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | TYR60 |
A | HOH626 |
B | PRO429 |
B | HOH643 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 505 |
Chain | Residue |
A | SER179 |
A | ALA180 |
A | ARG184 |
A | NDP502 |
C | ALA180 |
C | ARG184 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue CL A 506 |
Chain | Residue |
A | ARG181 |
A | ARG184 |
C | ARG184 |
site_id | AC7 |
Number of Residues | 36 |
Details | binding site for residue FAD B 501 |
Chain | Residue |
B | ASN245 |
B | GLY278 |
B | ASP279 |
B | PRO295 |
B | LEU296 |
B | ALA297 |
B | THR298 |
B | ALA300 |
B | NDP502 |
B | HOH611 |
B | HOH618 |
B | HOH622 |
B | HOH635 |
A | PHE422 |
A | HOH648 |
B | GLY7 |
B | THR9 |
B | HIS10 |
B | ALA11 |
B | TYR31 |
B | GLU32 |
B | ARG33 |
B | ASN34 |
B | SER41 |
B | CSO42 |
B | HIS77 |
B | ASN78 |
B | VAL79 |
B | THR110 |
B | SER111 |
B | GLY112 |
B | SER113 |
B | CYS131 |
B | LYS132 |
B | ILE158 |
B | PHE242 |
site_id | AC8 |
Number of Residues | 21 |
Details | binding site for residue NDP B 502 |
Chain | Residue |
A | GLN423 |
B | ALA155 |
B | GLY156 |
B | TYR157 |
B | ILE158 |
B | GLU161 |
B | ARG178 |
B | SER179 |
B | ARG184 |
B | LYS185 |
B | TYR186 |
B | CYS239 |
B | ILE240 |
B | GLY241 |
B | PHE242 |
B | PRO295 |
B | LEU296 |
B | SER325 |
B | GLY326 |
B | FAD501 |
B | HOH623 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
B | ARG332 |
B | MET390 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue EDO B 504 |
Chain | Residue |
A | PRO429 |
B | PHE14 |
B | TYR60 |
B | HOH636 |
site_id | AD2 |
Number of Residues | 34 |
Details | binding site for residue FAD C 501 |
Chain | Residue |
C | GLY7 |
C | CYS8 |
C | THR9 |
C | HIS10 |
C | ALA11 |
C | GLU32 |
C | ARG33 |
C | ASN34 |
C | SER41 |
C | CSO42 |
C | HIS77 |
C | ASN78 |
C | VAL79 |
C | THR110 |
C | SER111 |
C | GLY112 |
C | SER113 |
C | CYS131 |
C | LYS132 |
C | ILE158 |
C | PHE242 |
C | ASN245 |
C | LEU248 |
C | GLY278 |
C | ASP279 |
C | LEU296 |
C | ALA297 |
C | THR298 |
C | ALA300 |
C | NDP502 |
C | HOH620 |
C | HOH636 |
C | HOH641 |
D | PHE422 |
site_id | AD3 |
Number of Residues | 18 |
Details | binding site for residue NDP C 502 |
Chain | Residue |
C | GLY154 |
C | ALA155 |
C | GLY156 |
C | TYR157 |
C | ILE158 |
C | GLU161 |
C | ALA177 |
C | ARG178 |
C | SER179 |
C | TYR186 |
C | CYS239 |
C | ILE240 |
C | GLY241 |
C | PRO295 |
C | LEU296 |
C | GLY326 |
C | FAD501 |
D | GLN423 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue EDO C 503 |
Chain | Residue |
C | ARG332 |
C | GLU357 |
C | PRO370 |
C | MET390 |
C | SER391 |
C | HOH627 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue EDO C 504 |
Chain | Residue |
C | ARG428 |
C | PRO429 |
C | HOH640 |
site_id | AD6 |
Number of Residues | 35 |
Details | binding site for residue FAD D 501 |
Chain | Residue |
C | PHE422 |
C | GLN423 |
D | GLY7 |
D | CYS8 |
D | THR9 |
D | HIS10 |
D | ALA11 |
D | GLU32 |
D | ARG33 |
D | ASN34 |
D | SER41 |
D | CSO42 |
D | HIS77 |
D | ASN78 |
D | VAL79 |
D | THR110 |
D | SER111 |
D | GLY112 |
D | SER113 |
D | CYS131 |
D | LYS132 |
D | PHE242 |
D | LEU248 |
D | GLY278 |
D | ASP279 |
D | PRO295 |
D | LEU296 |
D | ALA297 |
D | ALA300 |
D | NDP502 |
D | HOH613 |
D | HOH630 |
D | HOH635 |
D | HOH637 |
D | HOH652 |
site_id | AD7 |
Number of Residues | 18 |
Details | binding site for residue NDP D 502 |
Chain | Residue |
C | HOH609 |
D | ALA155 |
D | GLY156 |
D | TYR157 |
D | ILE158 |
D | ARG178 |
D | SER179 |
D | ARG184 |
D | LYS185 |
D | TYR186 |
D | ILE240 |
D | GLY241 |
D | PHE242 |
D | PRO295 |
D | LEU296 |
D | SER325 |
D | GLY326 |
D | FAD501 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue EDO D 503 |
Chain | Residue |
C | PHE14 |
C | TYR60 |
D | ARG428 |
D | PRO429 |
D | HOH645 |
site_id | AD9 |
Number of Residues | 3 |
Details | binding site for residue EDO D 504 |
Chain | Residue |
D | ARG332 |
D | MET390 |
D | SER391 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue CL D 505 |
Chain | Residue |
B | ARG184 |
D | ARG181 |