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: |
Chain | Residue | Details |
A | ASP447 | |
D | ASP447 | |
D | ASN474 | |
D | GLN476 | |
A | ASN474 | |
A | GLN476 | |
B | ASP447 | |
B | ASN474 | |
B | GLN476 | |
C | ASP447 | |
C | ASN474 | |
C | GLN476 |
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 | 8 |
Details | M-CSA 274 |
Chain | Residue | Details |
A | GLU59 | 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 | GLU59 | 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 |
site_id | MCSA3 |
Number of Residues | 8 |
Details | M-CSA 274 |
Chain | Residue | Details |
C | GLU59 | activator, hydrogen bond acceptor, increase acidity, proton acceptor, proton donor |
C | PHE121 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
C | GLN122 | activator, electrostatic destabiliser, hydrogen bond acceptor, hydrogen bond donor, promote heterolysis |
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 | 8 |
Details | M-CSA 274 |
Chain | Residue | Details |
D | GLU59 | activator, hydrogen bond acceptor, increase acidity, proton acceptor, proton donor |
D | PHE121 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
D | GLN122 | activator, electrostatic destabiliser, hydrogen bond acceptor, hydrogen bond donor, promote heterolysis |
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 |