3DVA
Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004739 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004739 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0004739 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004739 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| E | 0004739 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004739 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| G | 0004739 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) activity |
| G | 0005515 | molecular_function | protein binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0004739 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) activity |
| H | 0005515 | molecular_function | protein binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| I | 0004742 | molecular_function | dihydrolipoyllysine-residue acetyltransferase activity |
| I | 0005515 | molecular_function | protein binding |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0016746 | molecular_function | acyltransferase activity |
| J | 0004742 | molecular_function | dihydrolipoyllysine-residue acetyltransferase activity |
| J | 0005515 | molecular_function | protein binding |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0016746 | molecular_function | acyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A1368 |
| Chain | Residue |
| A | ASP173 |
| A | ASN202 |
| A | PHE204 |
| A | TPW1370 |
| A | HOH1410 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B1325 |
| Chain | Residue |
| B | ASP165 |
| B | HOH1363 |
| B | ILE112 |
| B | THR113 |
| B | ALA160 |
| B | ASP163 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A1326 |
| Chain | Residue |
| A | HOH1421 |
| B | HOH1335 |
| C | HOH1420 |
| C | HOH1483 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C1368 |
| Chain | Residue |
| C | ASP173 |
| C | ASN202 |
| C | PHE204 |
| C | TPW1370 |
| C | HOH1432 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K D1325 |
| Chain | Residue |
| D | ILE112 |
| D | THR113 |
| D | ALA160 |
| D | ASP163 |
| D | ASP165 |
| D | HOH1474 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG G 369 |
| Chain | Residue |
| G | ASP173 |
| G | ASN202 |
| G | PHE204 |
| G | TPW1370 |
| G | HOH1407 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 369 |
| Chain | Residue |
| E | GLY172 |
| E | ASP173 |
| E | GLN200 |
| E | ASN202 |
| E | PHE204 |
| E | TPW1370 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 370 |
| Chain | Residue |
| E | HOH1466 |
| F | HOH1358 |
| G | HOH1410 |
| H | HOH1480 |
| H | HOH1481 |
| site_id | AC9 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPW A1370 |
| Chain | Residue |
| A | TYR102 |
| A | ARG103 |
| A | ILE142 |
| A | ILE144 |
| A | GLY172 |
| A | ASP173 |
| A | GLY174 |
| A | GLY175 |
| A | GLN178 |
| A | ASN202 |
| A | PHE204 |
| A | ALA205 |
| A | ARG267 |
| A | HIS271 |
| A | MG1368 |
| A | HOH1410 |
| A | HOH1412 |
| A | HOH1463 |
| A | HOH1482 |
| A | HOH1493 |
| D | GLU28 |
| D | LEU57 |
| D | GLU59 |
| D | GLN81 |
| D | PHE85 |
| site_id | BC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE TPW C1370 |
| Chain | Residue |
| B | GLU28 |
| B | LEU57 |
| B | GLU59 |
| B | GLN81 |
| B | PHE85 |
| C | TYR102 |
| C | ARG103 |
| C | ILE142 |
| C | ILE144 |
| C | GLY172 |
| C | ASP173 |
| C | GLY174 |
| C | GLY175 |
| C | GLN178 |
| C | ASN202 |
| C | PHE204 |
| C | ALA205 |
| C | ALA206 |
| C | HIS271 |
| C | MG1368 |
| C | HOH1382 |
| C | HOH1394 |
| C | HOH1413 |
| C | HOH1432 |
| C | HOH1444 |
| C | HOH1455 |
| site_id | BC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TPW E1370 |
| Chain | Residue |
| E | GLY174 |
| E | GLY175 |
| E | GLN178 |
| E | ASN202 |
| E | PHE204 |
| E | ALA205 |
| E | ALA206 |
| E | HIS271 |
| E | MG369 |
| E | HOH1458 |
| E | HOH1478 |
| E | HOH1496 |
| H | GLU28 |
| H | LEU57 |
| H | GLU59 |
| H | GLN81 |
| H | PHE85 |
| E | TYR102 |
| E | ARG103 |
| E | ILE142 |
| E | ILE144 |
| E | GLY172 |
| E | ASP173 |
| site_id | BC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPW G1370 |
| Chain | Residue |
| F | GLU28 |
| F | LEU57 |
| F | GLU59 |
| F | GLN81 |
| F | PHE85 |
| G | TYR102 |
| G | ARG103 |
| G | ILE142 |
| G | ILE144 |
| G | GLY172 |
| G | ASP173 |
| G | GLY174 |
| G | GLY175 |
| G | GLN178 |
| G | ASN202 |
| G | PHE204 |
| G | ALA205 |
| G | ALA206 |
| G | HIS271 |
| G | MG369 |
| G | HOH1407 |
| G | HOH1408 |
| G | HOH1411 |
| G | HOH1459 |
| G | HOH1461 |
Functional Information from PROSITE/UniProt
| site_id | PS00189 |
| Number of Residues | 30 |
| Details | LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GdeVnedDVLceVQNdKAVveIpspvkGkV |
| Chain | Residue | Details |
| I | GLY27-VAL56 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255 |
| Chain | Residue | Details |
| I | HIS399 | |
| J | HIS399 | |
| F | GLU59 | |
| H | GLU59 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-lipoyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:8445635 |
| Chain | Residue | Details |
| I | LYS43 | |
| J | LYS43 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | HIS271 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| D | GLU59 | |
| D | HIS128 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| F | GLU59 | |
| F | HIS128 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| H | GLU59 | |
| H | HIS128 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| C | HIS271 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| E | HIS271 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| G | HIS271 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | GLU59 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| D | GLU59 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| F | GLU59 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| H | GLU59 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | GLU59 | |
| B | HIS128 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 106 |
| Chain | Residue | Details |
| B | GLU59 | proton acceptor, proton donor |
| B | HIS128 | proton acceptor, proton donor |
| A | TYR281 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 106 |
| Chain | Residue | Details |
| D | GLU59 | proton acceptor, proton donor |
| D | HIS128 | proton acceptor, proton donor |
| C | TYR281 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 2 |
| Details | M-CSA 106 |
| Chain | Residue | Details |
| F | GLU59 | proton acceptor, proton donor |
| F | HIS128 | proton acceptor, proton donor |
| E | TYR281 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 2 |
| Details | M-CSA 106 |
| Chain | Residue | Details |
| H | GLU59 | proton acceptor, proton donor |
| H | HIS128 | proton acceptor, proton donor |
| G | TYR281 | electrostatic stabiliser, hydrogen bond donor |
