1Y9D
Pyruvate Oxidase variant V265A from Lactobacillus plantarum
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 |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0030976 | molecular_function | thiamine pyrophosphate binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047112 | molecular_function | pyruvate oxidase activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0030976 | molecular_function | thiamine pyrophosphate binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047112 | molecular_function | pyruvate oxidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 2601 |
| Chain | Residue |
| A | ASP447 |
| A | ASN474 |
| A | GLN476 |
| A | TPP2602 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2604 |
| Chain | Residue |
| C | SER82 |
| C | HOH2843 |
| C | HOH2868 |
| C | HOH2896 |
| C | HOH2938 |
| C | HOH2989 |
| A | ILE480 |
| A | TPP2602 |
| C | GLY34 |
| C | GLY35 |
| C | SER36 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 2605 |
| Chain | Residue |
| A | MET452 |
| A | GLN455 |
| A | HOH2858 |
| C | MET452 |
| C | GLN455 |
| C | HOH2859 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 2701 |
| Chain | Residue |
| B | ASP447 |
| B | ASN474 |
| B | GLN476 |
| B | TPP2702 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 D 2704 |
| Chain | Residue |
| B | ILE480 |
| B | TPP2702 |
| D | GLY34 |
| D | GLY35 |
| D | SER36 |
| D | SER82 |
| D | HOH2937 |
| D | HOH2978 |
| D | HOH3054 |
| D | HOH3072 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 2705 |
| Chain | Residue |
| B | MET452 |
| B | GLN455 |
| B | HOH2971 |
| D | MET452 |
| D | GLN455 |
| D | HOH2971 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 2801 |
| Chain | Residue |
| C | ASP447 |
| C | ASN474 |
| C | GLN476 |
| C | TPP2802 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2804 |
| Chain | Residue |
| A | GLY34 |
| A | GLY35 |
| A | SER36 |
| A | SER82 |
| A | HOH2827 |
| A | HOH2832 |
| A | HOH2977 |
| A | HOH3050 |
| C | ILE480 |
| C | TPP2802 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 2901 |
| Chain | Residue |
| D | ASP447 |
| D | ASN474 |
| D | GLN476 |
| D | TPP2902 |
| D | HOH2946 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2904 |
| Chain | Residue |
| B | GLY34 |
| B | GLY35 |
| B | SER36 |
| B | SER82 |
| B | PHE111 |
| B | HOH2937 |
| B | HOH2939 |
| B | HOH3108 |
| B | HOH3151 |
| D | ILE480 |
| D | TPP2902 |
| site_id | BC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP A 2602 |
| Chain | Residue |
| 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 | MG2601 |
| A | HOH2843 |
| A | HOH2846 |
| A | HOH2882 |
| C | PRO33 |
| C | GLU59 |
| C | SER82 |
| C | PRO85 |
| C | HIS89 |
| C | SO42604 |
| C | HOH2896 |
| site_id | BC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE FAD A 2603 |
| Chain | Residue |
| A | THR244 |
| A | PRO246 |
| A | GLY284 |
| A | ASN285 |
| A | ASN286 |
| A | ASP306 |
| A | ILE307 |
| A | LYS311 |
| A | ASP325 |
| A | ALA326 |
| A | HOH2901 |
| A | GLY220 |
| A | ILE221 |
| A | GLY222 |
| site_id | BC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TPP B 2702 |
| Chain | Residue |
| B | VAL394 |
| B | ASP396 |
| B | ALA420 |
| B | MET422 |
| B | ASP447 |
| B | GLY448 |
| B | GLY449 |
| B | ASN474 |
| B | GLN476 |
| B | TYR477 |
| B | GLY478 |
| B | PHE479 |
| B | ILE480 |
| B | MG2701 |
| B | HOH2906 |
| B | HOH2915 |
| B | HOH3007 |
| D | PRO33 |
| D | GLU59 |
| D | SER82 |
| D | PRO85 |
| D | HIS89 |
| D | SO42704 |
| D | HOH2978 |
| site_id | BC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FAD B 2703 |
| Chain | Residue |
| B | GLY220 |
| B | ILE221 |
| B | GLY222 |
| B | THR244 |
| B | PRO246 |
| B | GLY284 |
| B | ASN285 |
| B | ASN286 |
| B | ASP306 |
| B | ILE307 |
| B | ASP308 |
| B | LYS311 |
| B | ALA324 |
| B | ASP325 |
| B | ALA326 |
| B | HOH2953 |
| B | HOH3059 |
| B | HOH3379 |
| site_id | BC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE TPP C 2802 |
| Chain | Residue |
| A | PRO33 |
| A | GLU59 |
| A | SER82 |
| A | PRO85 |
| A | HIS89 |
| A | SO42804 |
| A | HOH2832 |
| C | VAL394 |
| C | GLY395 |
| C | ASP396 |
| C | ALA420 |
| C | MET422 |
| C | GLY446 |
| C | ASP447 |
| C | GLY448 |
| C | GLY449 |
| C | ASN474 |
| C | GLN476 |
| C | TYR477 |
| C | GLY478 |
| C | PHE479 |
| C | ILE480 |
| C | MG2801 |
| C | HOH2848 |
| C | HOH2854 |
| C | HOH2855 |
| site_id | BC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FAD C 2803 |
| Chain | Residue |
| C | GLY220 |
| C | ILE221 |
| C | GLY222 |
| C | THR244 |
| C | PRO246 |
| C | GLY284 |
| C | ASN285 |
| C | ASN286 |
| C | ASP306 |
| C | ILE307 |
| C | LYS311 |
| C | ALA324 |
| C | ASP325 |
| C | ALA326 |
| C | HOH2931 |
| C | HOH3007 |
| C | HOH3015 |
| site_id | BC8 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE TPP D 2902 |
| Chain | Residue |
| B | PRO33 |
| B | GLU59 |
| B | SER82 |
| B | PRO85 |
| B | HIS89 |
| B | SO42904 |
| B | HOH2937 |
| D | VAL394 |
| D | ASP396 |
| D | ALA420 |
| D | MET422 |
| D | GLY446 |
| D | ASP447 |
| D | GLY448 |
| D | GLY449 |
| D | ASN474 |
| D | GLN476 |
| D | TYR477 |
| D | GLY478 |
| D | PHE479 |
| D | ILE480 |
| D | MG2901 |
| D | HOH2907 |
| D | HOH2946 |
| D | HOH2947 |
| D | HOH2976 |
| site_id | BC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FAD D 2903 |
| Chain | Residue |
| D | GLY220 |
| D | ILE221 |
| D | GLY222 |
| D | THR244 |
| D | PRO246 |
| D | GLY284 |
| D | ASN285 |
| D | ASN286 |
| D | ASP306 |
| D | ILE307 |
| D | ASP308 |
| D | LYS311 |
| D | ALA324 |
| D | ASP325 |
| D | ALA326 |
| D | HOH3020 |
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 | 12 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | ALA552 |
| site_id | CSA10 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | MET561 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| C | MET561 |
| site_id | CSA12 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| D | MET561 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | ALA552 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| C | ALA552 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| D | ALA552 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | ARG264 | |
| A | PHE479 | |
| A | GLU483 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | ARG264 | |
| B | PHE479 | |
| B | GLU483 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| C | ARG264 | |
| C | PHE479 | |
| C | GLU483 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| D | ARG264 | |
| D | PHE479 | |
| D | GLU483 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | MET561 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 274 |
| Chain | Residue | Details |
| A | GLU59 | activator, hydrogen bond acceptor, increase acidity, proton acceptor, proton donor |
| 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 | 7 |
| Details | M-CSA 274 |
| Chain | Residue | Details |
| B | GLU59 | activator, hydrogen bond acceptor, increase acidity, proton acceptor, proton donor |
| 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 |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 274 |
| Chain | Residue | Details |
| C | GLU59 | activator, hydrogen bond acceptor, increase acidity, proton acceptor, proton donor |
| C | ARG264 | radical stabiliser |
| C | VAL394 | polar/non-polar interaction, promote heterolysis, radical stabiliser, steric role |
| C | PHE479 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
| C | ILE480 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
| C | GLU483 | radical stabiliser |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 274 |
| Chain | Residue | Details |
| D | GLU59 | activator, hydrogen bond acceptor, increase acidity, proton acceptor, proton donor |
| D | ARG264 | radical stabiliser |
| D | VAL394 | polar/non-polar interaction, promote heterolysis, radical stabiliser, steric role |
| D | PHE479 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
| D | ILE480 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
| D | GLU483 | radical stabiliser |
