6HAF
Pyruvate oxidase variant E59Q from L. plantarum in complex with phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047112 | molecular_function | pyruvate oxidase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047112 | molecular_function | pyruvate oxidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | binding site for residue FAD A 701 |
| Chain | Residue |
| A | HIS101 |
| A | ARG264 |
| A | VAL265 |
| A | GLY284 |
| A | ASN285 |
| A | ASN286 |
| A | TYR287 |
| A | PRO288 |
| A | PHE289 |
| A | ASP306 |
| A | ILE307 |
| A | PHE121 |
| A | ASP308 |
| A | LYS311 |
| A | ALA324 |
| A | ASP325 |
| A | ALA326 |
| A | ASN398 |
| A | SER416 |
| A | ASN417 |
| A | HOH806 |
| A | HOH889 |
| A | GLY220 |
| A | HOH963 |
| A | HOH1002 |
| A | HOH1023 |
| A | HOH1141 |
| A | HOH1272 |
| A | HOH1311 |
| A | ILE221 |
| A | GLY222 |
| A | THR244 |
| A | TYR245 |
| A | ALA262 |
| A | ASN263 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue K A 702 |
| Chain | Residue |
| A | MET452 |
| A | MET452 |
| A | GLN455 |
| A | GLN455 |
| A | HOH984 |
| A | HOH984 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 703 |
| Chain | Residue |
| A | ASP447 |
| A | ASN474 |
| A | GLN476 |
| A | TPP704 |
| A | HOH868 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | binding site for residue TPP A 704 |
| Chain | Residue |
| A | PRO33 |
| A | GLN59 |
| A | SER82 |
| A | PRO85 |
| A | HIS89 |
| A | GLN122 |
| A | VAL394 |
| A | ASP396 |
| A | ALA420 |
| A | MET422 |
| A | GLY446 |
| A | ASP447 |
| A | GLY448 |
| A | GLY449 |
| A | ASN474 |
| A | GLN476 |
| A | TYR477 |
| A | GLY478 |
| A | PHE479 |
| A | ILE480 |
| A | MG703 |
| A | PO4712 |
| A | HOH840 |
| A | HOH868 |
| A | HOH897 |
| A | HOH924 |
| A | HOH1049 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 705 |
| Chain | Residue |
| A | ALA23 |
| A | TRP24 |
| A | LYS75 |
| A | TYR158 |
| A | ALA186 |
| A | TYR189 |
| A | HOH913 |
| A | HOH1241 |
| B | HOH900 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 706 |
| Chain | Residue |
| A | LYS433 |
| A | PRO437 |
| A | GLU438 |
| A | PRO466 |
| A | ALA533 |
| A | GLN534 |
| A | HOH820 |
| A | HOH1061 |
| A | HOH1184 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 707 |
| Chain | Residue |
| A | TRP174 |
| A | THR487 |
| A | GLN489 |
| A | HOH1165 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 708 |
| Chain | Residue |
| A | HOH1082 |
| A | HOH1142 |
| A | HOH1209 |
| A | ARG264 |
| A | GLU483 |
| A | ASP486 |
| A | GLU553 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 709 |
| Chain | Residue |
| A | SER410 |
| A | ARG412 |
| A | TYR436 |
| A | ARG439 |
| A | HOH895 |
| A | HOH1438 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 710 |
| Chain | Residue |
| A | ARG224 |
| A | PRO409 |
| A | ASN411 |
| A | ARG412 |
| A | HOH895 |
| A | HOH907 |
| A | HOH932 |
| A | HOH1177 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 711 |
| Chain | Residue |
| A | ILE54 |
| A | LEU434 |
| A | TYR463 |
| A | HOH1208 |
| B | GLU341 |
| B | HOH1127 |
| site_id | AD3 |
| Number of Residues | 13 |
| Details | binding site for residue PO4 A 712 |
| Chain | Residue |
| A | GLY34 |
| A | GLY35 |
| A | SER36 |
| A | SER82 |
| A | PHE111 |
| A | GLN122 |
| A | ILE480 |
| A | TPP704 |
| A | HOH821 |
| A | HOH840 |
| A | HOH841 |
| A | HOH856 |
| A | HOH1230 |
| site_id | AD4 |
| Number of Residues | 35 |
| Details | binding site for residue FAD B 701 |
| Chain | Residue |
| B | HIS101 |
| B | PHE121 |
| B | GLY220 |
| B | ILE221 |
| B | GLY222 |
| B | THR244 |
| B | TYR245 |
| B | ALA262 |
| B | ASN263 |
| B | ARG264 |
| B | VAL265 |
| B | GLY284 |
| B | ASN285 |
| B | ASN286 |
| B | TYR287 |
| B | PRO288 |
| B | PHE289 |
| B | ASP306 |
| B | ILE307 |
| B | ASP308 |
| B | LYS311 |
| B | ALA324 |
| B | ASP325 |
| B | ALA326 |
| B | ASN398 |
| B | SER416 |
| B | ASN417 |
| B | HOH875 |
| B | HOH946 |
| B | HOH982 |
| B | HOH1003 |
| B | HOH1072 |
| B | HOH1115 |
| B | HOH1186 |
| B | HOH1310 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue K B 702 |
| Chain | Residue |
| B | MET452 |
| B | MET452 |
| B | GLN455 |
| B | GLN455 |
| B | HOH972 |
| B | HOH972 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 703 |
| Chain | Residue |
| B | ASP447 |
| B | ASN474 |
| B | GLN476 |
| B | TPP704 |
| B | HOH862 |
| site_id | AD7 |
| Number of Residues | 26 |
| Details | binding site for residue TPP B 704 |
| Chain | Residue |
| B | PRO33 |
| B | GLN59 |
| B | SER82 |
| B | PRO85 |
| B | HIS89 |
| B | VAL394 |
| B | ASP396 |
| B | ALA420 |
| B | MET422 |
| B | GLY446 |
| B | ASP447 |
| B | GLY448 |
| B | GLY449 |
| B | ASN474 |
| B | GLN476 |
| B | TYR477 |
| B | GLY478 |
| B | PHE479 |
| B | ILE480 |
| B | MG703 |
| B | PO4710 |
| B | HOH862 |
| B | HOH885 |
| B | HOH924 |
| B | HOH997 |
| B | HOH1082 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 705 |
| Chain | Residue |
| A | HOH850 |
| B | ALA569 |
| B | PHE570 |
| B | ARG573 |
| B | TYR574 |
| B | HOH952 |
| B | HOH1047 |
| site_id | AD9 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 706 |
| Chain | Residue |
| B | LYS433 |
| B | PRO437 |
| B | GLU438 |
| B | PRO466 |
| B | ALA533 |
| B | GLN534 |
| B | HOH826 |
| B | HOH854 |
| B | HOH953 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 707 |
| Chain | Residue |
| B | SER410 |
| B | ARG412 |
| B | TYR436 |
| B | ARG439 |
| B | HOH813 |
| B | HOH820 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 708 |
| Chain | Residue |
| B | ARG224 |
| B | PRO409 |
| B | HOH813 |
| B | HOH904 |
| B | HOH978 |
| site_id | AE3 |
| Number of Residues | 12 |
| Details | binding site for residue GOL B 709 |
| Chain | Residue |
| B | GLY25 |
| B | ASP27 |
| B | HIS28 |
| B | ASP69 |
| B | THR73 |
| B | LYS75 |
| B | ILE76 |
| B | ASN435 |
| B | HOH808 |
| B | HOH821 |
| B | HOH979 |
| B | HOH1103 |
| site_id | AE4 |
| Number of Residues | 12 |
| Details | binding site for residue PO4 B 710 |
| Chain | Residue |
| B | GLY34 |
| B | GLY35 |
| B | SER36 |
| B | SER82 |
| B | PHE111 |
| B | GLN122 |
| B | ILE480 |
| B | TPP704 |
| B | HOH842 |
| B | HOH855 |
| B | HOH885 |
| B | HOH887 |
Functional Information from PROSITE/UniProt
| site_id | PS00187 |
| Number of Residues | 20 |
| Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IAaklnyPerqvFnLaGDGG |
| Chain | Residue | Details |
| A | ILE430-GLY449 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP447 | |
| A | ASN474 | |
| A | GLN476 | |
| B | ASP447 | |
| B | ASN474 | |
| B | GLN476 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 274 |
| Chain | Residue | Details |
| A | GLN59 | activator, hydrogen bond acceptor, increase acidity, proton acceptor, proton donor |
| A | PHE121 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
| A | GLN122 | activator, electrostatic destabiliser, hydrogen bond acceptor, hydrogen bond donor, promote heterolysis |
| A | ARG264 | radical stabiliser |
| A | VAL394 | polar/non-polar interaction, promote heterolysis, radical stabiliser, steric role |
| A | PHE479 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
| A | ILE480 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
| A | GLU483 | radical stabiliser |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 274 |
| Chain | Residue | Details |
| B | GLN59 | activator, hydrogen bond acceptor, increase acidity, proton acceptor, proton donor |
| B | PHE121 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
| B | GLN122 | activator, electrostatic destabiliser, hydrogen bond acceptor, hydrogen bond donor, promote heterolysis |
| B | ARG264 | radical stabiliser |
| B | VAL394 | polar/non-polar interaction, promote heterolysis, radical stabiliser, steric role |
| B | PHE479 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
| B | ILE480 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
| B | GLU483 | radical stabiliser |
