2GF3
Structure of the complex of monomeric sarcosine with its substrate analogue inhibitor 2-furoic acid at 1.3 A resolution.
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 | 6 |
| Details | BINDING SITE FOR RESIDUE CL A 403 |
| Chain | Residue |
| A | TYR317 |
| A | THR318 |
| A | SER343 |
| A | GLY344 |
| A | FAD400 |
| A | HOH502 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 405 |
| Chain | Residue |
| A | HOH464 |
| A | HOH853 |
| A | HIS81 |
| A | ASN151 |
| A | ARG154 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL B 403 |
| Chain | Residue |
| B | TYR317 |
| B | THR318 |
| B | PHE342 |
| B | SER343 |
| B | GLY344 |
| B | FAD400 |
| B | HOH486 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 405 |
| Chain | Residue |
| B | HIS53 |
| B | LEU113 |
| B | THR114 |
| B | GLU141 |
| B | PRO142 |
| B | ASN143 |
| B | SER144 |
| B | HOH464 |
| B | HOH713 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 406 |
| Chain | Residue |
| B | HIS81 |
| B | ASN151 |
| B | ARG154 |
| B | HOH427 |
| B | HOH717 |
| site_id | AC6 |
| 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 | 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 | FOA401 |
| A | CL403 |
| A | HOH408 |
| A | HOH411 |
| A | HOH424 |
| A | HOH434 |
| A | HOH476 |
| A | HOH825 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FOA A 401 |
| Chain | Residue |
| A | ILE50 |
| A | ARG52 |
| A | TYR254 |
| A | GLY344 |
| A | HIS345 |
| A | LYS348 |
| A | FAD400 |
| A | HOH825 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FOA B 402 |
| Chain | Residue |
| B | PRO217 |
| B | GLN219 |
| B | TYR221 |
| B | LYS319 |
| B | THR320 |
| B | LEU321 |
| B | HOH439 |
| B | HOH747 |
| B | HOH850 |
| site_id | AC9 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD B 400 |
| Chain | Residue |
| 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 |
| B | PHE342 |
| B | GLY344 |
| B | HIS345 |
| B | GLY346 |
| B | PHE347 |
| B | LYS348 |
| B | FOA401 |
| B | CL403 |
| B | HOH410 |
| B | HOH412 |
| B | HOH422 |
| B | HOH425 |
| B | HOH433 |
| B | GLY10 |
| B | GLY12 |
| B | SER13 |
| B | MET14 |
| B | VAL32 |
| B | ASP33 |
| B | ALA34 |
| B | PHE35 |
| B | HIS39 |
| B | GLY42 |
| B | SER43 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FOA B 401 |
| Chain | Residue |
| B | ILE50 |
| B | ARG52 |
| B | TYR254 |
| B | GLY344 |
| B | HIS345 |
| B | LYS348 |
| B | FAD400 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FOA A 402 |
| Chain | Residue |
| A | PRO217 |
| A | GLN219 |
| A | TYR221 |
| A | LYS319 |
| A | THR320 |
| A | HOH437 |
| A | HOH746 |
| A | HOH884 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 404 |
| Chain | Residue |
| A | GLU78 |
| A | LEU159 |
| A | HOH462 |
| B | LYS86 |
| B | ASN237 |
| B | ASP240 |
| B | HOH456 |
| B | HOH485 |
| B | HOH600 |
| B | HOH612 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | ASN237 |
| A | ASP240 |
| A | HOH468 |
| A | HOH469 |
| A | HOH572 |
| A | HOH795 |
| B | GLU78 |
| B | LEU159 |
| B | HOH579 |
| B | HOH597 |
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 | 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 |
