2GB0
Monomeric sarcosine oxidase: structure of a covalently flavinylated amine oxidizing enzyme
Replaces: 1L9FReplaces: 1B3MFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005829 | cellular_component | cytosol |
| A | 0008115 | molecular_function | sarcosine oxidase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0033514 | biological_process | L-lysine catabolic process to acetyl-CoA via L-pipecolate |
| A | 0050031 | molecular_function | L-pipecolate oxidase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0051698 | molecular_function | saccharopine oxidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005829 | cellular_component | cytosol |
| B | 0008115 | molecular_function | sarcosine oxidase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0033514 | biological_process | L-lysine catabolic process to acetyl-CoA via L-pipecolate |
| B | 0050031 | molecular_function | L-pipecolate oxidase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0051698 | molecular_function | saccharopine oxidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 801 |
| Chain | Residue |
| A | HIS81 |
| A | ASN151 |
| A | ARG154 |
| A | HOH840 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 802 |
| Chain | Residue |
| B | HOH1127 |
| A | THR2 |
| A | LYS28 |
| B | SER1 |
| B | HOH1018 |
| B | HOH1064 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 803 |
| Chain | Residue |
| A | THR318 |
| A | GLY344 |
| A | FAD400 |
| A | HOH1109 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 804 |
| Chain | Residue |
| B | HIS81 |
| B | ASN151 |
| B | ARG154 |
| B | HOH807 |
| B | HOH965 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 805 |
| Chain | Residue |
| B | HIS53 |
| B | LEU113 |
| B | THR114 |
| B | VAL115 |
| B | GLU141 |
| B | PRO142 |
| B | ASN143 |
| B | SER144 |
| B | HOH917 |
| B | HOH1129 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 806 |
| Chain | Residue |
| B | TYR317 |
| B | THR318 |
| B | GLY344 |
| B | FAD400 |
| B | HOH1099 |
| site_id | AC7 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD A 400 |
| 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 | THR171 |
| A | ARG172 |
| A | VAL173 |
| A | SER200 |
| A | MET201 |
| A | GLY202 |
| A | TRP204 |
| A | LEU208 |
| A | TYR254 |
| A | CYS315 |
| A | MET316 |
| A | TYR317 |
| A | PHE342 |
| A | GLY344 |
| A | HIS345 |
| A | GLY346 |
| A | PHE347 |
| A | LYS348 |
| A | CL803 |
| A | HOH809 |
| A | HOH824 |
| A | HOH825 |
| A | HOH873 |
| A | HOH894 |
| A | HOH896 |
| site_id | AC8 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD B 400 |
| Chain | Residue |
| B | PHE342 |
| B | GLY344 |
| B | HIS345 |
| B | GLY346 |
| B | PHE347 |
| B | LYS348 |
| B | CL806 |
| B | HOH812 |
| B | HOH814 |
| B | HOH825 |
| B | HOH836 |
| B | HOH838 |
| B | HOH998 |
| 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 | TYR254 |
| B | CYS315 |
| B | MET316 |
| B | TYR317 |
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 | a catalytic site defined by CSA, PubMed 10368302, 16878980 |
| Chain | Residue | Details |
| A | HIS269 | |
| A | CYS315 | |
| A | ARG49 | |
| A | HIS45 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 10368302, 16878980 |
| Chain | Residue | Details |
| B | HIS269 | |
| B | CYS315 | |
| B | ARG49 | |
| B | HIS45 |
| 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 |
