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THE REFINED STRUCTURES OF A STABILIZED MUTANT AND OF WILD-TYPE PYRUVATE OXIDASE 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 610 |
| Chain | Residue |
| A | ASP447 |
| A | ASN474 |
| A | GLN476 |
| A | TPP611 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 610 |
| Chain | Residue |
| B | ASP447 |
| B | ASN474 |
| B | GLN476 |
| B | TPP611 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE TPP A 611 |
| Chain | Residue |
| A | GLU59 |
| A | SER82 |
| A | PRO85 |
| A | HIS89 |
| A | GLN122 |
| A | ASP396 |
| A | ALA420 |
| A | MET422 |
| A | ASP447 |
| A | GLY448 |
| A | GLY449 |
| A | ASN474 |
| A | GLN476 |
| A | TYR477 |
| A | GLY478 |
| A | PHE479 |
| A | ILE480 |
| A | MG610 |
| A | HOH617 |
| A | HOH659 |
| A | HOH664 |
| A | PRO33 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD A 612 |
| Chain | Residue |
| A | HIS101 |
| A | PHE121 |
| A | GLY220 |
| A | ILE221 |
| A | GLY222 |
| A | THR244 |
| A | TYR245 |
| A | ALA262 |
| A | ASN263 |
| A | ARG264 |
| A | VAL265 |
| A | GLY284 |
| A | ASN285 |
| A | ASN286 |
| A | TYR287 |
| A | PRO288 |
| A | PHE289 |
| A | ASP306 |
| A | ILE307 |
| A | LYS311 |
| A | ASP325 |
| A | ALA326 |
| A | ASN398 |
| A | SER416 |
| A | ASN417 |
| A | HOH614 |
| A | HOH635 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TPP B 611 |
| Chain | Residue |
| B | PRO33 |
| B | GLU59 |
| B | SER82 |
| B | PRO85 |
| B | HIS89 |
| B | GLN122 |
| B | ASP396 |
| B | ALA420 |
| B | MET422 |
| B | GLY446 |
| B | ASP447 |
| B | GLY448 |
| B | GLY449 |
| B | MET452 |
| B | ASN474 |
| B | GLN476 |
| B | TYR477 |
| B | GLY478 |
| B | PHE479 |
| B | ILE480 |
| B | MG610 |
| B | HOH635 |
| B | HOH651 |
| B | HOH662 |
| site_id | AC6 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD B 612 |
| Chain | Residue |
| B | ASP306 |
| B | ILE307 |
| B | LYS311 |
| B | ASP325 |
| B | ALA326 |
| B | ASN398 |
| B | SER416 |
| B | ASN417 |
| B | HOH640 |
| B | HIS101 |
| B | PHE121 |
| B | GLY220 |
| B | ILE221 |
| B | GLY222 |
| B | THR244 |
| B | TYR245 |
| B | PRO246 |
| B | ALA262 |
| B | ASN263 |
| B | ARG264 |
| B | VAL265 |
| B | GLY284 |
| B | ASN285 |
| B | ASN286 |
| B | TYR287 |
| B | PRO288 |
| B | PHE289 |
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 | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 8145244, 8438155, 9582325 |
| Chain | Residue | Details |
| A | ARG264 | |
| A | PHE479 | |
| A | GLU483 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 8145244, 8438155, 9582325 |
| Chain | Residue | Details |
| B | ARG264 | |
| B | PHE479 | |
| B | GLU483 |
| 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 |
