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 | 0009083 | biological_process | branched-chain amino acid catabolic process |
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 | 0009083 | biological_process | branched-chain amino acid catabolic process |
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 | 0009083 | biological_process | branched-chain amino acid catabolic process |
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 | 0009083 | biological_process | branched-chain amino acid catabolic process |
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 | 0016407 | molecular_function | acetyltransferase activity |
I | 0016740 | molecular_function | transferase activity |
I | 0016746 | molecular_function | acyltransferase activity |
I | 0031405 | molecular_function | lipoic acid binding |
J | 0004742 | molecular_function | dihydrolipoyllysine-residue acetyltransferase activity |
J | 0005515 | molecular_function | protein binding |
J | 0005737 | cellular_component | cytoplasm |
J | 0016407 | molecular_function | acetyltransferase activity |
J | 0016740 | molecular_function | transferase activity |
J | 0016746 | molecular_function | acyltransferase activity |
J | 0031405 | molecular_function | lipoic acid binding |
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 | 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 |