2VVL
The structure of MAO-N-D3, a variant of monoamine oxidase from Aspergillus niger.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005777 | cellular_component | peroxisome |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0097621 | molecular_function | monoamine oxidase activity |
B | 0005777 | cellular_component | peroxisome |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0097621 | molecular_function | monoamine oxidase activity |
C | 0005777 | cellular_component | peroxisome |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0097621 | molecular_function | monoamine oxidase activity |
D | 0005777 | cellular_component | peroxisome |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0097621 | molecular_function | monoamine oxidase activity |
E | 0005777 | cellular_component | peroxisome |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0097621 | molecular_function | monoamine oxidase activity |
F | 0005777 | cellular_component | peroxisome |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0097621 | molecular_function | monoamine oxidase activity |
G | 0005777 | cellular_component | peroxisome |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0097621 | molecular_function | monoamine oxidase activity |
H | 0005777 | cellular_component | peroxisome |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0097621 | molecular_function | monoamine oxidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE FAD A 600 |
Chain | Residue |
A | ILE45 |
A | GLY76 |
A | ARG77 |
A | GLY91 |
A | GLY92 |
A | THR93 |
A | TRP94 |
A | PRO278 |
A | VAL279 |
A | THR307 |
A | ILE308 |
A | GLY46 |
A | PRO309 |
A | TRP420 |
A | PHE425 |
A | ALA429 |
A | TRP430 |
A | ASN456 |
A | SER457 |
A | SER465 |
A | PHE466 |
A | ILE467 |
A | GLY48 |
A | ALA470 |
A | HOH2005 |
A | HOH2083 |
A | HOH2107 |
A | HOH2113 |
A | HOH2118 |
A | TYR49 |
A | CYS50 |
A | GLU69 |
A | ALA70 |
A | ARG71 |
A | GLY75 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 601 |
Chain | Residue |
A | HIS112 |
A | ASN113 |
A | ALA114 |
A | LEU115 |
E | PHE170 |
E | ASP173 |
E | TYR176 |
site_id | AC3 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE FAD B 600 |
Chain | Residue |
B | ILE45 |
B | GLY46 |
B | GLY48 |
B | TYR49 |
B | CYS50 |
B | GLU69 |
B | ALA70 |
B | ARG71 |
B | GLY75 |
B | GLY76 |
B | ARG77 |
B | GLY91 |
B | GLY92 |
B | THR93 |
B | TRP94 |
B | PRO278 |
B | VAL279 |
B | THR307 |
B | PRO309 |
B | TRP420 |
B | PHE425 |
B | ALA429 |
B | TRP430 |
B | ASN456 |
B | SER457 |
B | SER465 |
B | PHE466 |
B | ILE467 |
B | ALA470 |
B | HOH2091 |
B | HOH2097 |
B | HOH2132 |
B | HOH2133 |
site_id | AC4 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD C 600 |
Chain | Residue |
C | SER457 |
C | SER465 |
C | PHE466 |
C | ILE467 |
C | ALA470 |
C | HOH2093 |
C | GLY46 |
C | GLY48 |
C | TYR49 |
C | CYS50 |
C | GLU69 |
C | ALA70 |
C | ARG71 |
C | GLY75 |
C | GLY76 |
C | ARG77 |
C | GLY91 |
C | GLY92 |
C | THR93 |
C | TRP94 |
C | PRO278 |
C | VAL279 |
C | THR307 |
C | ILE308 |
C | PRO309 |
C | TRP420 |
C | PHE425 |
C | ALA429 |
C | TRP430 |
C | ASN456 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 601 |
Chain | Residue |
C | ASN120 |
C | ARG123 |
C | ARG351 |
C | THR371 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 602 |
Chain | Residue |
B | PHE170 |
B | ASP173 |
B | TYR176 |
C | HIS112 |
C | ASN113 |
C | ALA114 |
C | LEU115 |
site_id | AC7 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD D 600 |
Chain | Residue |
D | ILE45 |
D | GLY46 |
D | GLY48 |
D | TYR49 |
D | CYS50 |
D | GLU69 |
D | ALA70 |
D | ARG71 |
D | GLY75 |
D | GLY76 |
D | ARG77 |
D | GLY91 |
D | GLY92 |
D | THR93 |
D | TRP94 |
D | PRO278 |
D | VAL279 |
D | THR307 |
D | ILE308 |
D | PRO309 |
D | ILE316 |
D | PHE425 |
D | ALA429 |
D | TRP430 |
D | ASN456 |
D | SER457 |
D | SER465 |
D | PHE466 |
D | ILE467 |
D | ALA470 |
D | HOH2098 |
D | HOH2102 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO D 601 |
Chain | Residue |
D | HIS112 |
D | ASN113 |
D | ALA114 |
D | LEU115 |
H | PHE170 |
H | ASP173 |
H | TYR176 |
site_id | AC9 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD E 600 |
Chain | Residue |
E | ILE45 |
E | GLY46 |
E | GLY48 |
E | TYR49 |
E | CYS50 |
E | GLU69 |
E | ALA70 |
E | ARG71 |
E | GLY75 |
E | GLY76 |
E | ARG77 |
E | GLY91 |
E | GLY92 |
E | THR93 |
E | TRP94 |
E | PRO278 |
E | VAL279 |
E | THR307 |
E | ILE308 |
E | PRO309 |
E | TRP420 |
E | PHE425 |
E | ALA429 |
E | TRP430 |
E | ASN456 |
E | SER457 |
E | SER465 |
E | PHE466 |
E | ILE467 |
E | ALA470 |
E | HOH2006 |
E | HOH2075 |
E | HOH2117 |
E | HOH2122 |
site_id | BC1 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD F 600 |
Chain | Residue |
F | ILE45 |
F | GLY46 |
F | GLY48 |
F | TYR49 |
F | CYS50 |
F | GLU69 |
F | ALA70 |
F | ARG71 |
F | GLY76 |
F | ARG77 |
F | GLY91 |
F | GLY92 |
F | THR93 |
F | TRP94 |
F | PRO278 |
F | VAL279 |
F | THR307 |
F | PRO309 |
F | TRP420 |
F | PHE425 |
F | TRP430 |
F | ASN456 |
F | SER457 |
F | SER465 |
F | PHE466 |
F | ILE467 |
F | ALA470 |
F | HOH2073 |
F | HOH2075 |
F | HOH2102 |
F | HOH2103 |
site_id | BC2 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD G 600 |
Chain | Residue |
G | GLY46 |
G | GLY48 |
G | TYR49 |
G | CYS50 |
G | GLU69 |
G | ALA70 |
G | ARG71 |
G | GLY75 |
G | GLY76 |
G | ARG77 |
G | GLY91 |
G | GLY92 |
G | THR93 |
G | TRP94 |
G | PRO278 |
G | VAL279 |
G | ILE308 |
G | PRO309 |
G | TRP420 |
G | PHE425 |
G | ALA429 |
G | TRP430 |
G | ASN456 |
G | SER457 |
G | SER465 |
G | PHE466 |
G | ILE467 |
G | ALA470 |
G | HOH2051 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO G 601 |
Chain | Residue |
F | ASN120 |
F | ARG123 |
F | ARG351 |
F | THR371 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO G 602 |
Chain | Residue |
F | HIS112 |
F | ASN113 |
F | ALA114 |
F | LEU115 |
G | PHE170 |
G | ASP173 |
G | TYR176 |
site_id | BC5 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD H 600 |
Chain | Residue |
H | ILE45 |
H | GLY46 |
H | GLY48 |
H | TYR49 |
H | CYS50 |
H | GLU69 |
H | ALA70 |
H | ARG71 |
H | GLY75 |
H | GLY76 |
H | ARG77 |
H | GLY91 |
H | GLY92 |
H | THR93 |
H | TRP94 |
H | PRO278 |
H | VAL279 |
H | THR307 |
H | ILE308 |
H | PRO309 |
H | TRP420 |
H | PHE425 |
H | ALA429 |
H | TRP430 |
H | ASN456 |
H | SER457 |
H | SER465 |
H | PHE466 |
H | ILE467 |
H | ALA470 |
H | HOH2058 |
H | HOH2075 |
H | HOH2079 |
H | HOH2080 |