1ELI
COMPLEX OF MONOMERIC SARCOSINE OXIDASE WITH THE INHIBITOR PYRROLE-2-CARBOXYLATE
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 803 |
| Chain | Residue |
| A | HIS81 |
| A | ASN151 |
| A | ARG154 |
| A | HOH901 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 804 |
| Chain | Residue |
| A | THR318 |
| A | PHE342 |
| A | SER343 |
| A | GLY344 |
| A | FAD400 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 812 |
| Chain | Residue |
| B | HIS53 |
| B | LEU113 |
| B | THR114 |
| B | VAL115 |
| B | GLU141 |
| B | PRO142 |
| B | ASN143 |
| B | SER144 |
| B | HOH911 |
| B | HOH1129 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 813 |
| Chain | Residue |
| B | HIS81 |
| B | ASN151 |
| B | ARG154 |
| B | HOH824 |
| B | HOH1115 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 814 |
| Chain | Residue |
| B | TYR317 |
| B | THR318 |
| B | GLY344 |
| B | FAD400 |
| B | HOH872 |
| site_id | AC6 |
| Number of Residues | 41 |
| Details | BINDING SITE FOR RESIDUE FAD A 400 |
| Chain | Residue |
| A | GLY10 |
| A | GLY12 |
| A | SER13 |
| A | MSE14 |
| 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 | MSE201 |
| A | GLY202 |
| A | TRP204 |
| A | LEU208 |
| A | VAL225 |
| A | TYR254 |
| A | CYS315 |
| A | MSE316 |
| A | TYR317 |
| A | PHE342 |
| A | GLY344 |
| A | HIS345 |
| A | GLY346 |
| A | PHE347 |
| A | LYS348 |
| A | PYC801 |
| A | CL804 |
| A | HOH814 |
| A | HOH820 |
| A | HOH825 |
| A | HOH858 |
| A | HOH889 |
| A | HOH934 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PYC A 801 |
| Chain | Residue |
| A | ILE50 |
| A | ARG52 |
| A | MSE245 |
| A | TYR254 |
| A | HIS269 |
| A | TYR317 |
| A | GLY344 |
| A | HIS345 |
| A | LYS348 |
| A | FAD400 |
| site_id | AC8 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD B 400 |
| Chain | Residue |
| B | GLY202 |
| B | TRP204 |
| B | LEU208 |
| B | VAL225 |
| B | TYR254 |
| B | CYS315 |
| B | MSE316 |
| B | TYR317 |
| B | PHE342 |
| B | GLY344 |
| B | HIS345 |
| B | GLY346 |
| B | PHE347 |
| B | LYS348 |
| B | PYC811 |
| B | CL814 |
| B | HOH821 |
| B | HOH823 |
| B | HOH826 |
| B | HOH827 |
| B | HOH868 |
| B | GLY10 |
| B | GLY12 |
| B | SER13 |
| B | MSE14 |
| 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 | MSE201 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PYC B 811 |
| Chain | Residue |
| B | ILE50 |
| B | ARG52 |
| B | MSE245 |
| B | TYR254 |
| B | HIS269 |
| B | TYR317 |
| B | GLY344 |
| B | HIS345 |
| B | LYS348 |
| B | FAD400 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PYC B 815 |
| Chain | Residue |
| B | PRO217 |
| B | GLN219 |
| B | TYR221 |
| B | LYS319 |
| B | THR320 |
| B | LEU321 |
| B | HOH936 |
| B | HOH1021 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"S-8alpha-FAD cysteine"} |
| Chain | Residue | Details |
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 | HIS53 | electrostatic stabiliser |
| A | GLY56 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | GLU57 | electrostatic stabiliser, modifies pKa |
| A | GLY285 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | GLU289 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ALA339 | activator, alter redox potential, covalently attached |
| A | ASN376 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 113 |
| Chain | Residue | Details |
| B | HIS53 | electrostatic stabiliser |
| B | GLY56 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | GLU57 | electrostatic stabiliser, modifies pKa |
| B | GLY285 | hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | GLU289 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ALA339 | activator, alter redox potential, covalently attached |
| B | ASN376 | electrostatic stabiliser, hydrogen bond donor |
