3M13
Crystal Structure of the Lys265Arg PEG-crystallized mutant of monomeric sarcosine oxidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0008115 | molecular_function | sarcosine oxidase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008115 | molecular_function | sarcosine oxidase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008115 | molecular_function | sarcosine oxidase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 37 |
| 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 | VAL225 |
| A | TYR254 |
| A | CYS315 |
| A | MET316 |
| A | TYR317 |
| A | PHE342 |
| A | GLY344 |
| A | HIS345 |
| A | SER13 |
| A | GLY346 |
| A | PHE347 |
| A | LYS348 |
| A | HOH394 |
| A | CL405 |
| A | HOH578 |
| A | HOH581 |
| A | HOH582 |
| A | MET14 |
| 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 | PHE342 |
| A | SER343 |
| A | GLY344 |
| A | FAD400 |
| site_id | AC3 |
| Number of Residues | 37 |
| 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 | VAL173 |
| B | SER200 |
| B | MET201 |
| B | GLY202 |
| 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 | HOH396 |
| B | HOH404 |
| B | CL405 |
| B | HOH410 |
| B | HOH459 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 405 |
| Chain | Residue |
| B | THR318 |
| B | PHE342 |
| B | SER343 |
| B | GLY344 |
| B | HOH395 |
| B | FAD400 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 390 |
| Chain | Residue |
| B | HIS53 |
| B | LEU113 |
| B | THR114 |
| B | GLU141 |
| B | PRO142 |
| B | ASN143 |
| B | SER144 |
| site_id | AC6 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD C 400 |
| Chain | Residue |
| C | ALA34 |
| C | PHE35 |
| C | HIS39 |
| C | GLY42 |
| C | SER43 |
| C | HIS44 |
| C | ARG49 |
| C | ILE50 |
| C | THR171 |
| C | ARG172 |
| C | VAL173 |
| C | SER200 |
| C | MET201 |
| C | GLY202 |
| C | TRP204 |
| C | VAL225 |
| C | TYR254 |
| C | CYS315 |
| C | MET316 |
| C | TYR317 |
| C | PHE342 |
| C | GLY344 |
| C | HIS345 |
| C | GLY346 |
| C | PHE347 |
| C | LYS348 |
| C | HOH393 |
| C | HOH397 |
| C | CL405 |
| C | HOH412 |
| C | HOH456 |
| C | GLY10 |
| C | GLY12 |
| C | SER13 |
| C | MET14 |
| C | VAL32 |
| C | ASP33 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL C 405 |
| Chain | Residue |
| C | TYR317 |
| C | THR318 |
| C | PHE342 |
| C | SER343 |
| C | GLY344 |
| C | FAD400 |
| C | HOH458 |
| site_id | AC8 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD D 400 |
| Chain | Residue |
| D | GLY10 |
| D | GLY12 |
| D | SER13 |
| D | MET14 |
| D | VAL32 |
| D | ASP33 |
| D | ALA34 |
| D | PHE35 |
| D | HIS39 |
| D | GLY42 |
| D | SER43 |
| D | HIS44 |
| D | ARG49 |
| D | ILE50 |
| D | THR171 |
| D | ARG172 |
| D | VAL173 |
| D | SER200 |
| D | MET201 |
| D | GLY202 |
| D | TRP204 |
| D | LEU208 |
| D | VAL225 |
| D | TYR254 |
| D | CYS315 |
| D | MET316 |
| D | TYR317 |
| D | PHE342 |
| D | GLY344 |
| D | HIS345 |
| D | GLY346 |
| D | PHE347 |
| D | LYS348 |
| D | CL405 |
| D | HOH430 |
| D | HOH435 |
| D | HOH487 |
| D | HOH528 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL D 405 |
| Chain | Residue |
| D | TYR317 |
| D | THR318 |
| D | PHE342 |
| D | SER343 |
| D | GLY344 |
| D | FAD400 |
| D | HOH401 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 D 390 |
| Chain | Residue |
| D | HIS53 |
| D | LEU113 |
| D | THR114 |
| D | GLU141 |
| D | PRO142 |
| D | ASN143 |
| D | SER144 |
| D | HOH446 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 120 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"S-8alpha-FAD cysteine"} |
| Chain | Residue | Details |
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 |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 113 |
| Chain | Residue | Details |
| C | HIS45 | electrostatic stabiliser |
| C | THR48 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| C | ARG49 | electrostatic stabiliser, modifies pKa |
| C | ARG265 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
| C | HIS269 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | CYS315 | activator, alter redox potential, covalently attached |
| C | LYS348 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 7 |
| Details | M-CSA 113 |
| Chain | Residue | Details |
| D | HIS45 | electrostatic stabiliser |
| D | THR48 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| D | ARG49 | electrostatic stabiliser, modifies pKa |
| D | ARG265 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
| D | HIS269 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | CYS315 | activator, alter redox potential, covalently attached |
| D | LYS348 | electrostatic stabiliser, hydrogen bond donor |
