2A89
Monomeric Sarcosine Oxidase: Structure of a covalently flavinylated amine oxidizing enzyme
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 | 9 |
Details | BINDING SITE FOR RESIDUE PO4 B 1401 |
Chain | Residue |
B | HIS53 |
B | LEU113 |
B | THR114 |
B | GLU141 |
B | PRO142 |
B | ASN143 |
B | SER144 |
B | HOH2477 |
B | HOH2782 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 1402 |
Chain | Residue |
A | TYR317 |
A | THR318 |
A | GLY344 |
A | FCG1400 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CL A 1403 |
Chain | Residue |
A | ASN293 |
A | HOH1420 |
A | HOH1481 |
B | ASN293 |
B | HOH2425 |
B | HOH2433 |
B | HOH2729 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL B 2402 |
Chain | Residue |
B | TYR317 |
B | THR318 |
B | SER343 |
B | GLY344 |
B | FCG2400 |
B | HOH2413 |
site_id | AC5 |
Number of Residues | 40 |
Details | BINDING SITE FOR RESIDUE FCG A 1400 |
Chain | Residue |
A | GLY10 |
A | GLY12 |
A | SER13 |
A | MET14 |
A | VAL32 |
A | ASP33 |
A | ALA34 |
A | PHE35 |
A | HIS39 |
A | GLY42 |
A | SER43 |
A | HIS44 |
A | ARG49 |
A | ILE50 |
A | ARG172 |
A | VAL173 |
A | SER200 |
A | MET201 |
A | GLY202 |
A | TRP204 |
A | LEU208 |
A | VAL225 |
A | TYR254 |
A | PHE256 |
A | CYS315 |
A | MET316 |
A | TYR317 |
A | PHE342 |
A | GLY344 |
A | HIS345 |
A | GLY346 |
A | PHE347 |
A | LYS348 |
A | CL1402 |
A | HOH1422 |
A | HOH1431 |
A | HOH1440 |
A | HOH1458 |
A | HOH1542 |
A | HOH1636 |
site_id | AC6 |
Number of Residues | 40 |
Details | BINDING SITE FOR RESIDUE FCG B 2400 |
Chain | Residue |
B | LYS348 |
B | CL2402 |
B | HOH2403 |
B | HOH2409 |
B | HOH2411 |
B | HOH2426 |
B | HOH2466 |
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 | LEU208 |
B | VAL225 |
B | TYR254 |
B | PHE256 |
B | CYS315 |
B | MET316 |
B | TYR317 |
B | PHE342 |
B | GLY344 |
B | HIS345 |
B | GLY346 |
B | PHE347 |
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 | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 2gb0 |
Chain | Residue | Details |
A | HIS269 | |
A | CYS315 | |
A | ARG49 | |
A | HIS45 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 2gb0 |
Chain | Residue | Details |
B | HIS269 | |
B | CYS315 | |
B | ARG49 | |
B | HIS45 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2gb0 |
Chain | Residue | Details |
A | GLY344 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2gb0 |
Chain | Residue | Details |
B | GLY344 |
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 | LYS265 | 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 | LYS265 | 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 |