Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0071949 | molecular_function | FAD binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0071949 | molecular_function | FAD binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0071949 | molecular_function | FAD binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD A 499 |
Chain | Residue |
A | CYS60 |
A | SER101 |
A | GLY123 |
A | ALA124 |
A | CYS125 |
A | VAL128 |
A | GLY129 |
A | GLY131 |
A | GLY132 |
A | LEU133 |
A | GLY138 |
A | ARG61 |
A | TYR139 |
A | GLY192 |
A | GLY193 |
A | GLY196 |
A | VAL198 |
A | TYR445 |
A | ASN447 |
A | VGP500 |
A | HOH506 |
A | HOH512 |
A | SER62 |
A | HOH521 |
A | HOH539 |
A | HOH596 |
A | GLY63 |
A | GLY64 |
A | HIS65 |
A | CYS66 |
A | PHE70 |
A | LEU82 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE VGP A 500 |
Chain | Residue |
A | HIS65 |
A | GLY67 |
A | ALA124 |
A | CYS125 |
A | TYR139 |
A | GLY140 |
A | PRO141 |
A | PHE265 |
A | GLN328 |
A | SER341 |
A | MET374 |
A | ASN376 |
A | SER402 |
A | TYR448 |
A | FAD499 |
A | HOH527 |
A | HOH590 |
site_id | AC3 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD B 499 |
Chain | Residue |
B | CYS60 |
B | ARG61 |
B | SER62 |
B | GLY63 |
B | GLY64 |
B | HIS65 |
B | CYS66 |
B | PHE70 |
B | LEU82 |
B | SER101 |
B | GLY123 |
B | ALA124 |
B | CYS125 |
B | VAL128 |
B | GLY129 |
B | GLY131 |
B | GLY132 |
B | LEU133 |
B | GLY138 |
B | TYR139 |
B | GLY192 |
B | GLY193 |
B | GLY196 |
B | VAL198 |
B | TYR445 |
B | ASN447 |
B | VGP500 |
B | HOH506 |
B | HOH525 |
B | HOH569 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE VGP B 500 |
Chain | Residue |
B | HIS65 |
B | GLY67 |
B | ALA124 |
B | CYS125 |
B | TYR139 |
B | GLY140 |
B | PRO141 |
B | PHE265 |
B | PHE269 |
B | GLN328 |
B | SER341 |
B | MET374 |
B | ASN376 |
B | SER402 |
B | TYR448 |
B | FAD499 |
B | HOH657 |
site_id | AC5 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD C 499 |
Chain | Residue |
C | GLY63 |
C | GLY64 |
C | HIS65 |
C | CYS66 |
C | PHE70 |
C | LEU82 |
C | SER101 |
C | GLY123 |
C | ALA124 |
C | CYS125 |
C | VAL128 |
C | GLY129 |
C | GLY131 |
C | GLY132 |
C | LEU133 |
C | TYR139 |
C | GLY192 |
C | GLY193 |
C | GLY196 |
C | VAL198 |
C | TYR445 |
C | ASN447 |
C | VGP500 |
C | HOH514 |
C | HOH518 |
C | HOH559 |
C | HOH560 |
C | CYS60 |
C | ARG61 |
C | SER62 |
site_id | AC6 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE VGP C 500 |
Chain | Residue |
C | HIS65 |
C | GLY67 |
C | ALA124 |
C | CYS125 |
C | TYR139 |
C | GLY140 |
C | PRO141 |
C | PHE265 |
C | MET281 |
C | GLN328 |
C | SER341 |
C | MET374 |
C | ASN376 |
C | SER402 |
C | PHE404 |
C | TYR448 |
C | FAD499 |
C | HOH531 |
C | HOH535 |
C | HOH538 |
C | HOH555 |
site_id | AC7 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD D 499 |
Chain | Residue |
D | CYS60 |
D | ARG61 |
D | SER62 |
D | GLY63 |
D | GLY64 |
D | HIS65 |
D | CYS66 |
D | PHE70 |
D | LEU82 |
D | SER101 |
D | GLY123 |
D | ALA124 |
D | CYS125 |
D | VAL128 |
D | GLY129 |
D | GLY131 |
D | GLY132 |
D | LEU133 |
D | GLY138 |
D | TYR139 |
D | GLY192 |
D | GLY193 |
D | GLY196 |
D | VAL198 |
D | TYR445 |
D | ASN447 |
D | VGP500 |
D | HOH573 |
D | HOH580 |
site_id | AC8 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE VGP D 500 |
Chain | Residue |
D | HIS65 |
D | ALA124 |
D | CYS125 |
D | TYR139 |
D | GLY140 |
D | PRO141 |
D | PHE265 |
D | PHE269 |
D | MET281 |
D | GLN328 |
D | VAL334 |
D | SER341 |
D | MET374 |
D | ASN376 |
D | SER402 |
D | TYR448 |
D | FAD499 |
D | HOH529 |
D | HOH596 |
Functional Information from PROSITE/UniProt
site_id | PS00862 |
Number of Residues | 34 |
Details | OX2_COVAL_FAD Oxygen oxidoreductases covalent FAD-binding site. PeefflpaTpdDVvasLqkavtegrg...VacrSGGH |
Chain | Residue | Details |
A | PRO32-HIS65 | |