2XLS
Joint-functions of protein residues and NADP(H) in oxygen-activation by flavin-containing monooxygenase: Asn78Lys mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0050661 | molecular_function | NADP binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0050661 | molecular_function | NADP binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0050661 | molecular_function | NADP binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004497 | molecular_function | monooxygenase activity |
D | 0004499 | molecular_function | N,N-dimethylaniline monooxygenase activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FAD A 500 |
Chain | Residue |
A | GLY14 |
A | TRP52 |
A | HIS68 |
A | SER70 |
A | MET71 |
A | SER77 |
A | LYS78 |
A | THR129 |
A | ALA130 |
A | VAL131 |
A | CYS166 |
A | GLY16 |
A | THR167 |
A | GLY168 |
A | PHE170 |
A | GLN323 |
A | SER326 |
A | PHE327 |
A | PHE330 |
A | HOH2003 |
A | PRO17 |
A | SER18 |
A | GLU43 |
A | LYS44 |
A | GLN45 |
A | GLY50 |
A | GLN51 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NAP A 501 |
Chain | Residue |
A | LYS78 |
A | PRO176 |
A | VAL208 |
A | SER210 |
A | SER211 |
A | TYR212 |
A | SER213 |
A | ARG234 |
A | THR235 |
A | ASN251 |
A | CYS276 |
A | THR277 |
A | GLY278 |
A | ASN296 |
A | ASP322 |
A | GLN323 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EPE A 1451 |
Chain | Residue |
A | ARG24 |
A | GLN27 |
A | GLU31 |
A | LYS118 |
A | ALA119 |
C | ASN295 |
site_id | AC4 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FAD B 500 |
Chain | Residue |
B | GLY14 |
B | GLY16 |
B | PRO17 |
B | SER18 |
B | GLU43 |
B | LYS44 |
B | GLN45 |
B | GLY50 |
B | GLN51 |
B | TRP52 |
B | HIS68 |
B | SER70 |
B | MET71 |
B | SER77 |
B | LYS78 |
B | THR129 |
B | ALA130 |
B | VAL131 |
B | CYS166 |
B | THR167 |
B | PHE170 |
B | PHE285 |
B | GLN323 |
B | SER326 |
B | PHE327 |
B | PHE330 |
B | HOH2007 |
site_id | AC5 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NAP B 501 |
Chain | Residue |
B | LYS78 |
B | PHE170 |
B | TYR174 |
B | PRO176 |
B | VAL208 |
B | SER210 |
B | SER211 |
B | TYR212 |
B | SER213 |
B | ARG234 |
B | THR235 |
B | ASN251 |
B | CYS276 |
B | THR277 |
B | GLY278 |
B | ASN296 |
B | ASP322 |
B | GLN323 |
B | HOH2004 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EPE B 1453 |
Chain | Residue |
B | ALA119 |
B | ARG24 |
B | GLN27 |
B | GLU31 |
B | LYS118 |
site_id | AC7 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FAD C 500 |
Chain | Residue |
C | GLY14 |
C | GLY16 |
C | PRO17 |
C | SER18 |
C | GLU43 |
C | LYS44 |
C | GLN45 |
C | GLY50 |
C | GLN51 |
C | TRP52 |
C | HIS68 |
C | SER70 |
C | MET71 |
C | SER77 |
C | LYS78 |
C | THR129 |
C | ALA130 |
C | VAL131 |
C | CYS166 |
C | THR167 |
C | GLY168 |
C | PHE170 |
C | GLN323 |
C | SER326 |
C | PHE327 |
C | PHE330 |
C | HOH2002 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NAP C 501 |
Chain | Residue |
C | LYS78 |
C | PRO176 |
C | VAL208 |
C | SER210 |
C | SER211 |
C | TYR212 |
C | SER213 |
C | ARG234 |
C | THR235 |
C | ASN251 |
C | CYS276 |
C | THR277 |
C | GLY278 |
C | ASN296 |
C | ASP322 |
C | GLN323 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG C 1453 |
Chain | Residue |
A | HIS94 |
C | ARG234 |
site_id | BC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FAD D 500 |
Chain | Residue |
D | GLY14 |
D | GLY16 |
D | PRO17 |
D | SER18 |
D | GLU43 |
D | LYS44 |
D | GLN45 |
D | GLY50 |
D | GLN51 |
D | TRP52 |
D | HIS68 |
D | MET71 |
D | SER77 |
D | LYS78 |
D | THR129 |
D | ALA130 |
D | VAL131 |
D | CYS166 |
D | THR167 |
D | GLY168 |
D | PHE170 |
D | GLN323 |
D | SER326 |
D | PHE327 |
D | PHE330 |
D | HOH2002 |
D | HOH2011 |
site_id | BC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE NAP D 501 |
Chain | Residue |
D | LYS78 |
D | TYR174 |
D | PRO176 |
D | VAL208 |
D | SER210 |
D | SER211 |
D | TYR212 |
D | SER213 |
D | ARG234 |
D | THR235 |
D | ASN251 |
D | CYS276 |
D | THR277 |
D | GLY278 |
D | ASN296 |
D | ASP322 |
D | GLN323 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EPE D 1453 |
Chain | Residue |
D | ARG24 |
D | GLN27 |
D | GLU31 |
D | LYS118 |
D | GLY120 |
D | LYS123 |