3EY9
Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006090 | biological_process | pyruvate metabolic process |
| A | 0008289 | molecular_function | lipid binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042867 | biological_process | pyruvate catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048039 | molecular_function | ubiquinone binding |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0052737 | molecular_function | pyruvate dehydrogenase (quinone) activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006090 | biological_process | pyruvate metabolic process |
| B | 0008289 | molecular_function | lipid binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042867 | biological_process | pyruvate catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048039 | molecular_function | ubiquinone binding |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0052737 | molecular_function | pyruvate dehydrogenase (quinone) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE TPP A 611 |
| Chain | Residue |
| A | GLY381 |
| A | ASN460 |
| A | VAL462 |
| A | LEU463 |
| A | GLY464 |
| A | MG616 |
| B | THR25 |
| B | GLU50 |
| B | SER73 |
| B | HIS80 |
| B | GLN113 |
| A | THR382 |
| B | SO4621 |
| A | PRO383 |
| A | GLY406 |
| A | MET408 |
| A | GLY432 |
| A | ASP433 |
| A | GLY434 |
| A | GLY435 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD A 612 |
| Chain | Residue |
| A | HIS92 |
| A | GLY209 |
| A | SER210 |
| A | GLY211 |
| A | ALA233 |
| A | LEU234 |
| A | ARG235 |
| A | GLY236 |
| A | THR251 |
| A | GLY252 |
| A | LEU253 |
| A | ILE254 |
| A | GLY273 |
| A | THR274 |
| A | GLN275 |
| A | PHE276 |
| A | PRO277 |
| A | TYR278 |
| A | ASP292 |
| A | ILE293 |
| A | ASN294 |
| A | SER297 |
| A | GLY310 |
| A | ASP311 |
| A | ILE312 |
| A | PHE403 |
| A | ASN404 |
| A | TYR549 |
| B | PHE112 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 621 |
| Chain | Residue |
| A | GLY26 |
| A | ASP27 |
| A | SER28 |
| A | CYS74 |
| A | GLN113 |
| B | TPP611 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 616 |
| Chain | Residue |
| A | ASP433 |
| A | PHE458 |
| A | ASN460 |
| A | VAL462 |
| A | TPP611 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE TPP B 611 |
| Chain | Residue |
| A | THR25 |
| A | GLU50 |
| A | SER73 |
| A | HIS80 |
| A | GLN113 |
| A | SO4621 |
| B | GLY381 |
| B | THR382 |
| B | PRO383 |
| B | GLY406 |
| B | MET408 |
| B | GLY432 |
| B | ASP433 |
| B | GLY434 |
| B | GLY435 |
| B | ASN460 |
| B | VAL462 |
| B | LEU463 |
| B | GLY464 |
| B | MG617 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD B 612 |
| Chain | Residue |
| B | ILE293 |
| B | ASN294 |
| B | SER297 |
| B | GLY310 |
| B | ASP311 |
| B | ILE312 |
| B | PHE403 |
| B | ASN404 |
| B | TYR549 |
| A | PHE112 |
| B | HIS92 |
| B | GLY209 |
| B | SER210 |
| B | GLY211 |
| B | ALA233 |
| B | LEU234 |
| B | ARG235 |
| B | GLY236 |
| B | THR251 |
| B | GLY252 |
| B | LEU253 |
| B | ILE254 |
| B | GLY273 |
| B | THR274 |
| B | GLN275 |
| B | PHE276 |
| B | TYR278 |
| B | ASP292 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 617 |
| Chain | Residue |
| B | ASP433 |
| B | PHE458 |
| B | ASN460 |
| B | VAL462 |
| B | TPP611 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 621 |
| Chain | Residue |
| A | TPP611 |
| B | GLY26 |
| B | ASP27 |
| B | SER28 |
| B | SER73 |
| B | CYS74 |
| B | GLN113 |
Functional Information from PROSITE/UniProt
| site_id | PS00187 |
| Number of Residues | 20 |
| Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. LGaqatePerqvVaMcGDGG |
| Chain | Residue | Details |
| A | LEU416-GLY435 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:18988747, ECO:0007744|PDB:3EY9, ECO:0007744|PDB:3EYA |
| Chain | Residue | Details |
| A | GLU50 | |
| B | THR274 | |
| B | ASP292 | |
| B | GLY406 | |
| B | ASP433 | |
| B | ASN460 | |
| A | THR251 | |
| A | THR274 | |
| A | ASP292 | |
| A | GLY406 | |
| A | ASP433 | |
| A | ASN460 | |
| B | GLU50 | |
| B | THR251 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18988747, ECO:0007744|PDB:3EY9, ECO:0007744|PDB:3EYA |
| Chain | Residue | Details |
| A | SER210 | |
| B | SER297 | |
| B | ASP311 | |
| B | THR382 | |
| B | PHE403 | |
| B | VAL462 | |
| A | LEU234 | |
| A | SER297 | |
| A | ASP311 | |
| A | THR382 | |
| A | PHE403 | |
| A | VAL462 | |
| B | SER210 | |
| B | LEU234 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Moves into active site upon enzyme activation, plays a role in electron transfer => ECO:0000255|HAMAP-Rule:MF_00850, ECO:0000269|PubMed:18988747 |
| Chain | Residue | Details |
| A | PHE465 | |
| B | PHE465 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: In vitro cleavage to yield alpha-peptide => ECO:0000269|PubMed:3902830 |
| Chain | Residue | Details |
| A | TYR549 | |
| B | TYR549 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 275 |
| Chain | Residue | Details |
| A | GLU50 | activator, hydrogen bond acceptor, hydrogen bond donor, increase acidity, promote heterolysis, proton acceptor, proton donor |
| A | PHE112 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
| A | GLN113 | hydrogen bond acceptor, promote heterolysis |
| A | VAL380 | electrostatic destabiliser, promote heterolysis, radical stabiliser, steric role, van der waals interaction |
| A | PHE465 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser, steric role |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 275 |
| Chain | Residue | Details |
| B | GLU50 | activator, hydrogen bond acceptor, hydrogen bond donor, increase acidity, promote heterolysis, proton acceptor, proton donor |
| B | PHE112 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser |
| B | GLN113 | hydrogen bond acceptor, promote heterolysis |
| B | VAL380 | electrostatic destabiliser, promote heterolysis, radical stabiliser, steric role, van der waals interaction |
| B | PHE465 | electrostatic destabiliser, polar/non-polar interaction, promote heterolysis, radical stabiliser, steric role |
