3M12
Crystal Structure of the Lys265Arg phosphate-crytsallized mutant of monomeric sarcosine oxidase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008115 | molecular_function | sarcosine oxidase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008115 | molecular_function | sarcosine oxidase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 41 |
Details | BINDING SITE FOR RESIDUE FAD A 400 |
Chain | Residue |
A | GLY10 |
A | GLY42 |
A | SER43 |
A | HIS44 |
A | ARG49 |
A | ILE50 |
A | THR171 |
A | ARG172 |
A | VAL173 |
A | SER200 |
A | MET201 |
A | GLY12 |
A | GLY202 |
A | TRP204 |
A | LEU208 |
A | GLN223 |
A | VAL225 |
A | TYR254 |
A | CYS315 |
A | MET316 |
A | TYR317 |
A | PHE342 |
A | SER13 |
A | GLY344 |
A | HIS345 |
A | GLY346 |
A | PHE347 |
A | LYS348 |
A | HOH390 |
A | CL405 |
A | HOH406 |
A | HOH428 |
A | HOH444 |
A | MET14 |
A | HOH462 |
A | HOH739 |
A | VAL32 |
A | ASP33 |
A | ALA34 |
A | PHE35 |
A | HIS39 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL A 405 |
Chain | Residue |
A | TYR317 |
A | THR318 |
A | SER343 |
A | GLY344 |
A | FAD400 |
A | HOH432 |
site_id | AC3 |
Number of Residues | 38 |
Details | BINDING SITE FOR RESIDUE FAD B 400 |
Chain | Residue |
B | GLY10 |
B | GLY12 |
B | SER13 |
B | MET14 |
B | VAL32 |
B | ASP33 |
B | ALA34 |
B | PHE35 |
B | HIS39 |
B | GLY42 |
B | SER43 |
B | HIS44 |
B | ARG49 |
B | ILE50 |
B | THR171 |
B | ARG172 |
B | VAL173 |
B | SER200 |
B | MET201 |
B | GLY202 |
B | TRP204 |
B | GLN223 |
B | TYR254 |
B | CYS315 |
B | MET316 |
B | TYR317 |
B | PHE342 |
B | GLY344 |
B | HIS345 |
B | GLY346 |
B | PHE347 |
B | LYS348 |
B | HOH397 |
B | HOH398 |
B | HOH399 |
B | CL406 |
B | HOH409 |
B | HOH711 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CL B 406 |
Chain | Residue |
B | TYR317 |
B | THR318 |
B | PHE342 |
B | SER343 |
B | GLY344 |
B | FAD400 |
B | HOH412 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | ASP5 | |
B | ASP5 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: S-8alpha-FAD cysteine |
Chain | Residue | Details |
A | CYS315 | |
B | CYS315 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 113 |
Chain | Residue | Details |
A | HIS45 | electrostatic stabiliser |
A | THR48 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | ARG49 | electrostatic stabiliser, modifies pKa |
A | ARG265 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | HIS269 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | CYS315 | activator, alter redox potential, covalently attached |
A | LYS348 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 113 |
Chain | Residue | Details |
B | HIS45 | electrostatic stabiliser |
B | THR48 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | ARG49 | electrostatic stabiliser, modifies pKa |
B | ARG265 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | HIS269 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | CYS315 | activator, alter redox potential, covalently attached |
B | LYS348 | electrostatic stabiliser, hydrogen bond donor |