1EL7
COMPLEX OF MONOMERIC SARCOSINE OXIDASE WITH THE INHIBITOR [METHYTELLURO]ACETATE
Functional 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 | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 803 |
| Chain | Residue |
| A | HIS81 |
| A | ASN151 |
| A | ARG154 |
| A | HOH878 |
| A | HOH1147 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 804 |
| Chain | Residue |
| A | FAD400 |
| A | TYR317 |
| A | THR318 |
| A | SER343 |
| A | GLY344 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 812 |
| Chain | Residue |
| B | HIS53 |
| B | LEU113 |
| B | THR114 |
| B | GLU141 |
| B | ASN143 |
| B | SER144 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 813 |
| Chain | Residue |
| B | HIS81 |
| B | ASN151 |
| B | ARG154 |
| B | HOH837 |
| B | HOH968 |
| B | HOH1054 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 814 |
| Chain | Residue |
| B | TYR317 |
| B | THR318 |
| B | SER343 |
| B | GLY344 |
| B | FAD400 |
| B | HOH826 |
| site_id | AC6 |
| Number of Residues | 41 |
| 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 | VAL225 |
| A | TYR254 |
| A | CYS315 |
| A | MET316 |
| A | TYR317 |
| A | PHE342 |
| A | GLY344 |
| A | HIS345 |
| A | GLY346 |
| A | PHE347 |
| A | LYS348 |
| A | MTD801 |
| A | CL804 |
| A | HOH811 |
| A | HOH821 |
| A | HOH833 |
| A | HOH855 |
| A | HOH871 |
| A | HOH912 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MTD A 801 |
| Chain | Residue |
| A | ILE50 |
| A | ARG52 |
| A | MET245 |
| A | TYR254 |
| A | HIS269 |
| A | TYR317 |
| A | GLY344 |
| A | LYS348 |
| A | FAD400 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE TE A 805 |
| Chain | Residue |
| A | CYS262 |
| site_id | AC9 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD B 400 |
| Chain | Residue |
| B | TRP204 |
| B | LEU208 |
| B | VAL225 |
| B | TYR254 |
| B | CYS315 |
| B | MET316 |
| B | TYR317 |
| B | PHE342 |
| B | GLY344 |
| B | HIS345 |
| B | GLY346 |
| B | PHE347 |
| B | LYS348 |
| B | MTD811 |
| B | CL814 |
| B | HOH823 |
| B | HOH824 |
| B | HOH828 |
| B | HOH843 |
| B | HOH870 |
| 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 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MTD B 811 |
| Chain | Residue |
| B | ILE50 |
| B | ARG52 |
| B | MET245 |
| B | TYR254 |
| B | HIS269 |
| B | TYR317 |
| B | GLY344 |
| B | LYS348 |
| B | FAD400 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE TE B 815 |
| Chain | Residue |
| B | CYS262 |
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 |
